位置:首页 > 蛋白库 > KGD_MYCS2
KGD_MYCS2
ID   KGD_MYCS2               Reviewed;        1227 AA.
AC   A0R2B1; I7GDF5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Multifunctional 2-oxoglutarate metabolism enzyme;
DE   AltName: Full=2-hydroxy-3-oxoadipate synthase;
DE            Short=HOA synthase;
DE            Short=HOAS;
DE            EC=2.2.1.5;
DE   AltName: Full=2-oxoglutarate carboxy-lyase;
DE   AltName: Full=2-oxoglutarate decarboxylase;
DE   AltName: Full=Alpha-ketoglutarate decarboxylase;
DE            Short=KG decarboxylase;
DE            Short=KGD;
DE            EC=4.1.1.71;
DE   AltName: Full=Alpha-ketoglutarate-glyoxylate carboligase;
DE   Includes:
DE     RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE              Short=ODH E1 component;
DE              EC=1.2.4.2;
DE     AltName: Full=Alpha-ketoglutarate dehydrogenase E1 component;
DE              Short=KDH E1 component;
DE   Includes:
DE     RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE              EC=2.3.1.61;
DE     AltName: Full=2-oxoglutarate dehydrogenase complex E2 component;
DE              Short=ODH E2 component;
DE              Short=OGDC-E2;
DE     AltName: Full=Dihydrolipoamide succinyltransferase;
GN   Name=kgd; Synonyms=sucA; OrderedLocusNames=MSMEG_5049, MSMEI_4922;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION IN 2-OXOGLUTARATE DECARBOXYLATION, ACTIVITY REGULATION, KINETIC
RP   PARAMETERS, AND INTERACTION WITH GARA.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
RA   O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
RA   Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K., Alzari P.M.;
RT   "Regulation of glutamate metabolism by protein kinases in mycobacteria.";
RL   Mol. Microbiol. 70:1408-1423(2008).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 116-1227 IN COMPLEXES WITH
RP   THIAMINE PYROPHOSPHATE; ACETYL-COA; ENAMINE-THDP REACTION INTERMEDIATE AND
RP   MAGNESIUM, FUNCTION AS A MULTIFUNCTIONAL ENZYME, CATALYTIC ACTIVITY,
RP   COFACTOR, ACTIVITY REGULATION, SUBUNIT, PATHWAY, MUTAGENESIS OF HIS-539;
RP   HIS-579; HIS-747; ARG-781; HIS-1020; GLU-1034 AND ARG-1062, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=21867916; DOI=10.1016/j.chembiol.2011.06.004;
RA   Wagner T., Bellinzoni M., Wehenkel A., O'Hare H.M., Alzari P.M.;
RT   "Functional plasticity and allosteric regulation of alpha-ketoglutarate
RT   decarboxylase in central mycobacterial metabolism.";
RL   Chem. Biol. 18:1011-1020(2011).
CC   -!- FUNCTION: Shows three enzymatic activities that share a first common
CC       step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate,
CC       KG), leading to the formation of an enamine-thiamine-PP intermediate
CC       upon decarboxylation. Thus, displays KGD activity, catalyzing the
CC       decarboxylation from five-carbon 2-oxoglutarate to four-carbon
CC       succinate semialdehyde (SSA). Also catalyzes C-C bond formation between
CC       the activated aldehyde formed after decarboxylation of alpha-
CC       ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-
CC       3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-
CC       hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate
CC       dehydrogenase (ODH) complex, that catalyzes the overall conversion of
CC       2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG
CC       dehydrogenase reactions provide two alternative, tightly regulated,
CC       pathways connecting the oxidative and reductive branches of the TCA
CC       cycle. {ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:21867916}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate +
CC         CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5;
CC         Evidence={ECO:0000269|PubMed:21867916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde;
CC         Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71;
CC         Evidence={ECO:0000269|PubMed:21867916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC         COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000269|PubMed:21867916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC         Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000269|PubMed:21867916};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:21867916};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:21867916};
CC   -!- ACTIVITY REGULATION: Alpha-ketoglutarate dehydrogenase and
CC       decarboxylase activities are inhibited by unphosphorylated GarA, and
CC       allosterically activated by acetyl-CoA, the main substrate of the TCA
CC       cycle. Both the phosphoadenosine and acetyl moieties of acetyl-CoA are
CC       important for activation because neither CoA nor the synthetic compound
CC       S-(2-acetamidoethyl)-ethanethioate (which mimics the terminal acetyl-
CC       phosphopantetheine group of acetyl-CoA) has an activation effect.
CC       {ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:21867916}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.54 mM for alpha-ketoglutarate {ECO:0000269|PubMed:19019160};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from 2-oxoglutarate (transferase route): step 1/2.
CC       {ECO:0000269|PubMed:21867916}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC       CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC       {ECO:0000269|PubMed:21867916}.
CC   -!- SUBUNIT: Homodimer. Interacts with the FHA domain of unphosphorylated
CC       GarA. The 2-oxoglutarate dehydrogenase (ODH) complex contains multiple
CC       copies of three enzymatic components: 2-oxoglutarate dehydrogenase
CC       (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide
CC       dehydrogenase (E3). {ECO:0000269|PubMed:19019160,
CC       ECO:0000269|PubMed:21867916}.
CC   -!- DOMAIN: Is a fusion protein with two major domains exhibiting
CC       structural features of an E1 and E2 protein, and a short sequence
CC       stretch of E1 localized at the N-terminus, which is connected by a
CC       linker region to the rest of the protein. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show any ODH
CC       activity, in contrast to wild-type, demonstrating that this protein is
CC       part of a functional ODH complex in mycobacteria.
CC       {ECO:0000269|PubMed:21867916}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000480; ABK74238.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41366.1; -; Genomic_DNA.
DR   RefSeq; WP_011730279.1; NZ_SIJM01000019.1.
DR   RefSeq; YP_889299.1; NC_008596.1.
DR   PDB; 2XT6; X-ray; 2.74 A; A/B=116-1227.
DR   PDB; 2XTA; X-ray; 2.20 A; A/B/C/D=361-1227.
DR   PDB; 2Y0P; X-ray; 2.40 A; A/B/C/D=361-1227.
DR   PDB; 2YIC; X-ray; 1.96 A; A/B/C/D=361-1227.
DR   PDB; 2YID; X-ray; 2.25 A; A/B/C/D=361-1227.
DR   PDB; 3ZHQ; X-ray; 2.50 A; A/B/C/D=361-1227.
DR   PDB; 3ZHR; X-ray; 2.10 A; A/B/C/D=361-1227.
DR   PDB; 3ZHS; X-ray; 2.10 A; A/B/C/D=361-1227.
DR   PDB; 3ZHT; X-ray; 2.15 A; A/B/C/D=361-1227.
DR   PDB; 3ZHU; X-ray; 2.30 A; A/B/C/D=361-1227.
DR   PDB; 3ZHV; X-ray; 2.30 A; A/B/C/D=361-1227.
DR   PDB; 6I2Q; X-ray; 2.15 A; A=361-1227.
DR   PDB; 6I2R; X-ray; 2.20 A; A/C=361-1227.
DR   PDB; 6I2S; X-ray; 2.40 A; A=361-1227.
DR   PDB; 6R29; X-ray; 1.67 A; A/B=361-1227.
DR   PDB; 6R2A; X-ray; 1.70 A; A/B=361-1227.
DR   PDB; 6R2B; X-ray; 1.96 A; A/B/C/D=361-1227.
DR   PDB; 6R2C; X-ray; 2.09 A; A/B/C/D=361-1227.
DR   PDB; 6R2D; X-ray; 2.30 A; A/B/C/D=361-1227.
DR   PDBsum; 2XT6; -.
DR   PDBsum; 2XTA; -.
DR   PDBsum; 2Y0P; -.
DR   PDBsum; 2YIC; -.
DR   PDBsum; 2YID; -.
DR   PDBsum; 3ZHQ; -.
DR   PDBsum; 3ZHR; -.
DR   PDBsum; 3ZHS; -.
DR   PDBsum; 3ZHT; -.
DR   PDBsum; 3ZHU; -.
DR   PDBsum; 3ZHV; -.
DR   PDBsum; 6I2Q; -.
DR   PDBsum; 6I2R; -.
DR   PDBsum; 6I2S; -.
DR   PDBsum; 6R29; -.
DR   PDBsum; 6R2A; -.
DR   PDBsum; 6R2B; -.
DR   PDBsum; 6R2C; -.
DR   PDBsum; 6R2D; -.
DR   AlphaFoldDB; A0R2B1; -.
DR   SMR; A0R2B1; -.
DR   IntAct; A0R2B1; 1.
DR   STRING; 246196.MSMEI_4922; -.
DR   PRIDE; A0R2B1; -.
DR   EnsemblBacteria; ABK74238; ABK74238; MSMEG_5049.
DR   EnsemblBacteria; AFP41366; AFP41366; MSMEI_4922.
DR   GeneID; 66736369; -.
DR   KEGG; msg:MSMEI_4922; -.
DR   KEGG; msm:MSMEG_5049; -.
DR   PATRIC; fig|246196.19.peg.4927; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 29166at2; -.
DR   BRENDA; 4.1.1.71; 3512.
DR   SABIO-RK; A0R2B1; -.
DR   UniPathway; UPA00223; UER00997.
DR   UniPathway; UPA00223; UER01001.
DR   EvolutionaryTrace; A0R2B1; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0050439; F:2-hydroxy-3-oxoadipate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 3.40.50.11610; -; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Allosteric enzyme; Coiled coil;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
KW   Oxidoreductase; Reference proteome; Thiamine pyrophosphate; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..1227
FT                   /note="Multifunctional 2-oxoglutarate metabolism enzyme"
FT                   /id="PRO_0000310718"
FT   REGION          1..41
FT                   /note="2-oxoglutarate dehydrogenase E1, N-terminal part"
FT   REGION          23..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          42..88
FT                   /note="Linker"
FT   REGION          89..335
FT                   /note="Succinyltransferase E2"
FT   REGION          336..1227
FT                   /note="2-oxoglutarate dehydrogenase E1, C-terminal part"
FT   REGION          1089..1092
FT                   /note="Acetyl-CoA; allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:21867916,
FT                   ECO:0007744|PDB:2XTA"
FT   REGION          1149..1150
FT                   /note="Acetyl-CoA; allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:21867916,
FT                   ECO:0007744|PDB:2XTA"
FT   COILED          783..814
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        43..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..76
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        314
FT                   /note="Proton acceptor; for succinyltransferase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         539..540
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT   BINDING         579
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT   BINDING         604..606
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT   BINDING         604
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT   BINDING         645..647
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT   BINDING         645
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         678
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         680
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         952
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT   BINDING         1020
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT   BINDING         1038
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:21867916,
FT                   ECO:0007744|PDB:2XTA"
FT   BINDING         1054
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:21867916,
FT                   ECO:0007744|PDB:2XTA"
FT   BINDING         1142
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000269|PubMed:21867916,
FT                   ECO:0007744|PDB:2XTA"
FT   MUTAGEN         539
FT                   /note="H->A: Loss of KG decarboxylase activity."
FT                   /evidence="ECO:0000269|PubMed:21867916"
FT   MUTAGEN         579
FT                   /note="H->A: Loss of KG decarboxylase activity."
FT                   /evidence="ECO:0000269|PubMed:21867916"
FT   MUTAGEN         747
FT                   /note="H->A: 40-fold decrease in KG decarboxylase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:21867916"
FT   MUTAGEN         781
FT                   /note="R->A: Increase in KG decarboxylase activity."
FT                   /evidence="ECO:0000269|PubMed:21867916"
FT   MUTAGEN         1020
FT                   /note="H->A: Loss of KG decarboxylase activity."
FT                   /evidence="ECO:0000269|PubMed:21867916"
FT   MUTAGEN         1034
FT                   /note="E->A: Loss of activation by acetyl-CoA."
FT                   /evidence="ECO:0000269|PubMed:21867916"
FT   MUTAGEN         1062
FT                   /note="R->A: Loss of activation by acetyl-CoA."
FT                   /evidence="ECO:0000269|PubMed:21867916"
FT   STRAND          124..132
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           134..149
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           157..171
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   STRAND          178..189
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   STRAND          213..216
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           224..238
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   TURN            239..241
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   STRAND          275..280
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           294..300
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   STRAND          305..313
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   TURN            314..316
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           319..332
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           336..345
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           366..380
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           381..384
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:2YIC"
FT   TURN            401..403
FT                   /evidence="ECO:0007829|PDB:2XT6"
FT   HELIX           406..408
FT                   /evidence="ECO:0007829|PDB:2XTA"
FT   HELIX           412..416
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          417..423
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          426..431
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           432..443
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          444..450
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           457..467
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           476..499
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          500..502
FT                   /evidence="ECO:0007829|PDB:6R2C"
FT   HELIX           504..506
FT                   /evidence="ECO:0007829|PDB:2YIC"
FT   HELIX           514..527
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          531..536
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           542..548
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           554..562
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            567..570
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          571..573
FT                   /evidence="ECO:0007829|PDB:2YID"
FT   HELIX           577..579
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          582..587
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          589..592
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          594..599
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            606..608
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           609..624
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          630..632
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          637..644
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           645..650
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           652..658
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            659..662
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            664..666
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          672..677
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           686..689
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          691..694
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           697..702
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          706..710
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           714..731
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          735..740
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           753..755
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           758..764
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           770..780
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           786..808
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           822..824
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           837..846
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            858..860
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           861..873
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           878..891
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          895..900
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            901..905
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          913..916
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            918..920
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           926..931
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          942..947
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           953..965
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          969..974
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           978..984
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           985..990
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            991..994
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           995..999
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1006..1010
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1014..1016
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1025..1031
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   TURN            1034..1036
FT                   /evidence="ECO:0007829|PDB:6R2C"
FT   STRAND          1038..1040
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1045..1057
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1064..1068
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1071..1074
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1076..1078
FT                   /evidence="ECO:0007829|PDB:2Y0P"
FT   HELIX           1082..1086
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1092..1094
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1097..1100
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1106..1108
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1111..1115
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1119..1130
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1135..1145
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1148..1155
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1163..1171
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1174..1176
FT                   /evidence="ECO:0007829|PDB:6R2B"
FT   HELIX           1177..1187
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1189..1192
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1196..1200
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   STRAND          1204..1207
FT                   /evidence="ECO:0007829|PDB:6R29"
FT   HELIX           1211..1225
FT                   /evidence="ECO:0007829|PDB:6R29"
SQ   SEQUENCE   1227 AA;  135944 MW;  76C5BFFD1638A391 CRC64;
     MSSSPSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTTDSAS NGRTTTAAPV
     TPPTPAPAPA PEPKAAPKPA AKTEAKPAKP AKSATPAKGD ESQILRGAAA AVVKNMNASL
     EVPTATSVRA IPAKLMIDNR VVINNHLKRT RGGKISFTHL LGYAIVQAVK KFPNMNRHFA
     VVDGKPTAIT PAHTNLGLAI DLQGKDGNRS LVVAAIKRCE TMRFGQFIAA YEDIVRRARD
     GKLTAEDFSG VTISLTNPGT LGTVHSVPRL MQGQGAIIGA GAMEYPAEFQ GASEERIADL
     GIGKLITLTS TYDHRIIQGA ESGDFLRTIH QLLLDDDFFD EIFRELGIPY EPVRWRTDNP
     DSIEDKNARV IELIAAYRNR GHLMADIDPL RLDNTRFRSH PDLDVNSHGL TLWDLDREFK
     VDGFAGVQRK KLRDILSVLR DAYCRHVGVE YTHILEPEQQ RWIQERVETK HDKPTVAEQK
     YILSKLNAAE AFETFLQTKY VGQKRFSLEG AETVIPMMDA VIDQCAEHGL DEVVIAMPHR
     GRLNVLANIV GKPYSQIFSE FEGNLNPSQA HGSGDVKYHL GATGTYIQMF GDNDIEVSLT
     ANPSHLEAVD PVLEGLVRAK QDLLDTGEEG SDNRFSVVPL MLHGDAAFAG QGVVAETLNL
     ALLRGYRTGG TIHIVVNNQI GFTTAPTDSR SSEYCTDVAK MIGAPIFHVN GDDPEACAWV
     ARLAVDFRQA FKKDVVIDML CYRRRGHNEG DDPSMTQPYM YDVIDTKRGS RKAYTEALIG
     RGDISMKEAE DALRDYQGQL ERVFNEVREL EKHEIEPSES VEADQQIPSK LATAVDKAML
     QRIGDAHLAL PEGFTVHPRV RPVLEKRREM AYEGRIDWAF AELLALGSLI AEGKLVRLSG
     QDTQRGTFTQ RHAVIVDRKT GEEFTPLQLL ATNPDGTPTG GKFLVYNSAL SEFAAVGFEY
     GYSVGNPDAM VLWEAQFGDF VNGAQSIIDE FISSGEAKWG QLSDVVLLLP HGHEGQGPDH
     TSGRIERFLQ LWAEGSMTIA MPSTPANYFH LLRRHGKDGI QRPLIVFTPK SMLRNKAAVS
     DIRDFTESKF RSVLEEPMYT DGEGDRNKVT RLLLTSGKIY YELAARKAKE NREDVAIVRI
     EQLAPLPRRR LAETLDRYPN VKEKFWVQEE PANQGAWPSF GLTLPEILPD HFTGLKRISR
     RAMSAPSSGS SKVHAVEQQE ILDTAFG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024