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KGD_MYCVP
ID   KGD_MYCVP               Reviewed;        1243 AA.
AC   A1TDK2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
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; OrderedLocusNames=Mvan_4477;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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   -!- 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   -!- 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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
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. {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from 2-oxoglutarate (transferase route): step 1/2.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC       CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC   -!- SUBUNIT: Homodimer. The 2-oxoglutarate dehydrogenase (ODH) complex
CC       contains multiple copies of three enzymatic components: 2-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM15252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000511; ABM15252.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041306940.1; NC_008726.1.
DR   AlphaFoldDB; A1TDK2; -.
DR   SMR; A1TDK2; -.
DR   STRING; 350058.Mvan_4477; -.
DR   PRIDE; A1TDK2; -.
DR   EnsemblBacteria; ABM15252; ABM15252; Mvan_4477.
DR   KEGG; mva:Mvan_4477; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_11; -.
DR   OrthoDB; 29166at2; -.
DR   UniPathway; UPA00223; UER00997.
DR   UniPathway; UPA00223; UER01001.
DR   Proteomes; UP000009159; 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   3: Inferred from homology;
KW   Acyltransferase; Allosteric enzyme; Coiled coil; Decarboxylase; Lyase;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Oxidoreductase;
KW   Reference proteome; Thiamine pyrophosphate; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..1243
FT                   /note="Multifunctional 2-oxoglutarate metabolism enzyme"
FT                   /id="PRO_0000310725"
FT   REGION          1..40
FT                   /note="2-oxoglutarate dehydrogenase E1, N-terminal part"
FT   REGION          22..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..103
FT                   /note="Linker"
FT   REGION          104..353
FT                   /note="Succinyltransferase E2"
FT   REGION          354..1243
FT                   /note="2-oxoglutarate dehydrogenase E1, C-terminal part"
FT   REGION          1105..1108
FT                   /note="Acetyl-CoA; allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT   REGION          1165..1166
FT                   /note="Acetyl-CoA; allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT   COILED          799..831
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        55..69
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /note="Proton acceptor; for succinyltransferase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         557..558
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         597
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         622..624
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         622
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         661..663
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         661
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         694
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         696
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         968
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         1036
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         1054
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT   BINDING         1070
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT   BINDING         1158
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:A0R2B1"
SQ   SEQUENCE   1243 AA;  136980 MW;  88066C7C78C4835D CRC64;
     MNSPSPFGQN EWLVEEMYRK FREDPSSVDP SWHEFLVDYS PEPTNDAPAG NGKPAAAPTA
     PPEPASAPAP KPASTNGGAP PAKADTSTTR APEKKPEEKT SPAPKAKTAA PAGVSDDDET
     QVLRGAAAAV VKNMSASLDV PTATSVRAIP AKAMIDNRIV INNHLKRTRG GKISFTHLLG
     YAIVQAVKKF PNMNRHFAEI DGKPVAVTPA HTNLGLAIDL PGKDGKRSLV VAAIKNCETM
     HFGQFIAAYE DIVRRARDGK LTAEDFAGVT ISLTNPGTIG TVHSVPRLMK GQGAIVGAGA
     MEYPAEFQGA SEERIAELGV GKLMTLTSTY DHRIIQGAES GDFLRTIHTL LLDDEFYDEI
     FRELGIPHEP VRWRIDNPDS IEDKNARVIE LIAAYRNRGH LMADIDPLRL DKTRFRSHPD
     LDVNTHGLTL WDLDREFKVN GFAGKTHKKL RDILGLLRDA YCRHIGVEYT HILEPEQQQW
     LQERIEVKHE KPTVAEQKYI LSKLNAAEAF ETFLQTKYVG QKRFSLEGAE TVIPMMDAAI
     DQCAEHGLDE VVIGMPHRGR LNVLANIVGK PYSQIFTEFE GNLNPSQAHG SGDVKYHLGA
     NGTYIQMFGD NDIDVSLVAN PSHLEAVDPV LEGLVRAKQD ILDKGNGPDG FTVVPMMLHG
     DAAFAGQGVV AETLNLALLR GYRTGGTIHI IVNNQIGFTT SPYDSRSSEY CTDVAKMIGA
     PIFHVNGDDP EACVWVAKLA VDFRQKFKKD VVIDMLCYRR RGHNEGDDPS MTQPTMYDVI
     DTKRGVRKSY TEALIGRGDI SMKEAEDALR DYQGQLERVF NEVRELEKHA IAPSSSVESD
     QMVPAGMSTA VDKSLLARIG DAHLGYPDDF NVHPRVKPVL EKRREMAYEG KVDWAFAELL
     ALGTFLAEGK TIRFTGQDTR RGTFTQRHSV IIDRQTGREF TPLDLLTVDS DGNPTGGKFM
     AYDSALSEFA AVGFEYGYSV GNPNALVLWE AQFGDFVNGA QSIIDEFISS GEAKWGQLSD
     VVLLLPHGHE GQGPDHTSGR IERFLLLWAE GSMTIAMPST PANYFHLLRR HGLDGIHRPL
     IVFTPKSMLR NKAAVSDLKD FTEMKFRSVL EEPTYTEGTG DRSKAKRILL TSGKLYYELA
     ARKSKEGRDD VAILRLEQLA PLPKRRLAAT LDEYPNAEQY FWVQEEPANQ GAWPTLGLTL
     PEVLPEKLAG IKRISRRAMS APSSGSSKVH AVEQQEIIDE AFG
 
 
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