KGD_MYCTU
ID KGD_MYCTU Reviewed; 1231 AA.
AC P9WIS5; L0T8T9; O50463; Q7D8I9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Multifunctional 2-oxoglutarate metabolism enzyme;
DE AltName: Full=2-hydroxy-3-oxoadipate synthase {ECO:0000303|PubMed:20416504};
DE Short=HOA synthase {ECO:0000303|PubMed:20416504};
DE Short=HOAS;
DE EC=2.2.1.5 {ECO:0000269|PubMed:20416504};
DE AltName: Full=2-oxoglutarate carboxy-lyase;
DE AltName: Full=2-oxoglutarate decarboxylase;
DE AltName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000303|PubMed:16027371};
DE Short=KG decarboxylase;
DE Short=KGD;
DE EC=4.1.1.71 {ECO:0000269|PubMed:16027371};
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 {ECO:0000269|PubMed:21867916};
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 {ECO:0000269|PubMed:21867916};
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=Rv1248c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP LACK OF FUNCTION AS A 2-OXOGLUTARATE DEHYDROGENASE COMPONENT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16045627; DOI=10.1111/j.1365-2958.2005.04741.x;
RA Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C.;
RT "Mycobacterium tuberculosis appears to lack alpha-ketoglutarate
RT dehydrogenase and encodes pyruvate dehydrogenase in widely separated
RT genes.";
RL Mol. Microbiol. 57:859-868(2005).
RN [3]
RP FUNCTION AS A 2-OXOGLUTARATE DECARBOXYLASE, CATALYTIC ACTIVITY, COFACTOR,
RP AND KINETIC PARAMETERS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16027371; DOI=10.1073/pnas.0501605102;
RA Tian J., Bryk R., Itoh M., Suematsu M., Nathan C.;
RT "Variant tricarboxylic acid cycle in Mycobacterium tuberculosis:
RT identification of alpha-ketoglutarate decarboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10670-10675(2005).
RN [4]
RP INTERACTION WITH GARA.
RC STRAIN=ATCC 25618 / H37Rv;
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 DISRUPTION PHENOTYPE, AND ROLE IN TCA CYCLE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19936047; DOI=10.1371/journal.ppat.1000662;
RA Baughn A.D., Garforth S.J., Vilcheze C., Jacobs W.R. Jr.;
RT "An anaerobic-type alpha-ketoglutarate ferredoxin oxidoreductase completes
RT the oxidative tricarboxylic acid cycle of Mycobacterium tuberculosis.";
RL PLoS Pathog. 5:E1000662-E1000662(2009).
RN [6]
RP ACTIVITY REGULATION, AND INTERACTION WITH GARA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19318624; DOI=10.1126/scisignal.2000212;
RA Nott T.J., Kelly G., Stach L., Li J., Westcott S., Patel D., Hunt D.M.,
RA Howell S., Buxton R.S., O'Hare H.M., Smerdon S.J.;
RT "An intramolecular switch regulates phosphoindependent FHA domain
RT interactions in Mycobacterium tuberculosis.";
RL Sci. Signal. 2:RA12-RA12(2009).
RN [7]
RP FUNCTION AS A HOA SYNTHASE, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20416504; DOI=10.1016/j.chembiol.2010.03.009;
RA de Carvalho L.P., Zhao H., Dickinson C.E., Arango N.M., Lima C.D.,
RA Fischer S.M., Ouerfelli O., Nathan C., Rhee K.Y.;
RT "Activity-based metabolomic profiling of enzymatic function: identification
RT of Rv1248c as a mycobacterial 2-hydroxy-3-oxoadipate synthase.";
RL Chem. Biol. 17:323-332(2010).
RN [8]
RP FUNCTION AS A MULTIFUNCTIONAL ENZYME, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(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, which can endow M.tuberculosis with the metabolic plasticity
CC required for growth on diverse host-derived carbon sources. Appears to
CC play a predominant role in growth on carbohydrates as the sole carbon
CC source, and only a minimal role during growth on fatty acids.
CC {ECO:0000269|PubMed:16027371, ECO:0000269|PubMed:19936047,
CC ECO:0000269|PubMed:20416504, 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:20416504};
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:16027371};
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:16027371, ECO:0000269|PubMed:20416504};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:16027371, ECO:0000269|PubMed:20416504};
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:0000269|PubMed:19318624, ECO:0000269|PubMed:21867916}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.48 mM for 2-oxoglutarate {ECO:0000269|PubMed:16027371};
CC KM=0.196 mM for magnesium ions {ECO:0000269|PubMed:16027371};
CC KM=0.019 mM for thiamine pyrophosphate {ECO:0000269|PubMed:16027371};
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 (By similarity). The 2-oxoglutarate dehydrogenase
CC (ODH) complex contains multiple copies of three enzymatic components:
CC 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase
CC (E2) and lipoamide dehydrogenase (E3) (By similarity). Interacts with
CC the FHA domain of unphosphorylated GarA. {ECO:0000250,
CC ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19318624}.
CC -!- INTERACTION:
CC P9WIS5; P9WJA9: garA; NbExp=4; IntAct=EBI-6405560, EBI-6405522;
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: Attempts to disrupt Rv1248c in M.tuberculosis
CC H37Rv and Erdman strains by homologous recombination were unsuccessful,
CC raising the possibility that Rv1248c may be essential
CC (PubMed:20416504). However, deletion mutants were readily obtained in a
CC strain derived from H37Rv in PubMed:19936047. The mutant strain grows
CC as well as wild-type in medium containing both carbohydrates (dextrose
CC and glycerol) and fatty acids, under a CO(2) enriched atmosphere, but
CC shows a marked growth defect when grown in medium containing
CC carbohydrates as the sole carbon source in the presence of CO(2).
CC Simultaneous disruption of korAB and kgd results in strict dependence
CC upon the glyoxylate shunt for growth. Growth of the kgd mutant strain
CC on fatty acids as the sole carbon source is similar to that of the wild
CC type strain regardless of the presence of CO(2). But cells lacking both
CC korAB and kgd is significantly more retarded for growth on fatty acids
CC than is either korAB or kgd deleted mutant alone.
CC {ECO:0000269|PubMed:19936047, ECO:0000269|PubMed:20416504}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:9634230 and PubMed:12218036) annotated
CC as sucA because of sequence similarity, but this protein was shown
CC (PubMed:16045627) not to be able to serve as the E1 component of 2-
CC oxoglutarate dehydrogenase (ODH). However, it was later shown that this
CC protein does in fact sustain ODH activity (PubMed:21867916), and
CC requires specific activation by acetyl-CoA.
CC {ECO:0000305|PubMed:16045627, ECO:0000305|PubMed:21867916}.
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DR EMBL; AL123456; CCP44004.1; -; Genomic_DNA.
DR PIR; G70953; G70953.
DR RefSeq; NP_215764.2; NC_000962.3.
DR RefSeq; WP_003898790.1; NZ_NVQJ01000049.1.
DR AlphaFoldDB; P9WIS5; -.
DR SMR; P9WIS5; -.
DR IntAct; P9WIS5; 1.
DR STRING; 83332.Rv1248c; -.
DR PaxDb; P9WIS5; -.
DR DNASU; 887084; -.
DR GeneID; 887084; -.
DR KEGG; mtu:Rv1248c; -.
DR TubercuList; Rv1248c; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR OMA; RDSYCRT; -.
DR PhylomeDB; P9WIS5; -.
DR BioCyc; MetaCyc:G185E-5419-MON; -.
DR BRENDA; 2.2.1.5; 3445.
DR SABIO-RK; P9WIS5; -.
DR UniPathway; UPA00223; UER00997.
DR UniPathway; UPA00223; UER01001.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:MTBBASE.
DR GO; GO:0050439; F:2-hydroxy-3-oxoadipate synthase activity; IDA:MTBBASE.
DR GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IDA:MTBBASE.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:MTBBASE.
DR GO; GO:0006105; P:succinate metabolic process; IDA:MTBBASE.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:MTBBASE.
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 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..1231
FT /note="Multifunctional 2-oxoglutarate metabolism enzyme"
FT /id="PRO_0000310722"
FT REGION 1..41
FT /note="2-oxoglutarate dehydrogenase E1, N-terminal part"
FT REGION 38..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..88
FT /note="Linker"
FT REGION 89..337
FT /note="Succinyltransferase E2"
FT REGION 338..1231
FT /note="2-oxoglutarate dehydrogenase E1, C-terminal part"
FT REGION 1093..1096
FT /note="Acetyl-CoA; allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT REGION 1153..1154
FT /note="Acetyl-CoA; allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT COILED 787..817
FT /evidence="ECO:0000255"
FT ACT_SITE 316
FT /note="Proton acceptor; for succinyltransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 541..542
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 581
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 606..608
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 606
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 649..651
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 649
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 956
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 1024
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 1042
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT BINDING 1058
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:A0R2B1"
FT BINDING 1146
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:A0R2B1"
SQ SEQUENCE 1231 AA; 135902 MW; 96C255612BA12889 CRC64;
MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTSQPAA EPTRVTSPLV
AERAAAAAPQ APPKPADTAA AGNGVVAALA AKTAVPPPAE GDEVAVLRGA AAAVVKNMSA
SLEVPTATSV RAVPAKLLID NRIVINNQLK RTRGGKISFT HLLGYALVQA VKKFPNMNRH
YTEVDGKPTA VTPAHTNLGL AIDLQGKDGK RSLVVAGIKR CETMRFAQFV TAYEDIVRRA
RDGKLTTEDF AGVTISLTNP GTIGTVHSVP RLMPGQGAII GVGAMEYPAE FQGASEERIA
ELGIGKLITL TSTYDHRIIQ GAESGDFLRT IHELLLSDGF WDEVFRELSI PYLPVRWSTD
NPDSIVDKNA RVMNLIAAYR NRGHLMADTD PLRLDKARFR SHPDLEVLTH GLTLWDLDRV
FKVDGFAGAQ YKKLRDVLGL LRDAYCRHIG VEYAHILDPE QKEWLEQRVE TKHVKPTVAQ
QKYILSKLNA AEAFETFLQT KYVGQKRFSL EGAESVIPMM DAAIDQCAEH GLDEVVIGMP
HRGRLNVLAN IVGKPYSQIF TEFEGNLNPS QAHGSGDVKY HLGATGLYLQ MFGDNDIQVS
LTANPSHLEA VDPVLEGLVR AKQDLLDHGS IDSDGQRAFS VVPLMLHGDA AFAGQGVVAE
TLNLANLPGY RVGGTIHIIV NNQIGFTTAP EYSRSSEYCT DVAKMIGAPI FHVNGDDPEA
CVWVARLAVD FRQRFKKDVV IDMLCYRRRG HNEGDDPSMT NPYVYDVVDT KRGARKSYTE
ALIGRGDISM KEAEDALRDY QGQLERVFNE VRELEKHGVQ PSESVESDQM IPAGLATAVD
KSLLARIGDA FLALPNGFTA HPRVQPVLEK RREMAYEGKI DWAFGELLAL GSLVAEGKLV
RLSGQDSRRG TFSQRHSVLI DRHTGEEFTP LQLLATNSDG SPTGGKFLVY DSPLSEYAAV
GFEYGYTVGN PDAVVLWEAQ FGDFVNGAQS IIDEFISSGE AKWGQLSNVV LLLPHGHEGQ
GPDHTSARIE RFLQLWAEGS MTIAMPSTPS NYFHLLRRHA LDGIQRPLIV FTPKSMLRHK
AAVSEIKDFT EIKFRSVLEE PTYEDGIGDR NKVSRILLTS GKLYYELAAR KAKDNRNDLA
IVRLEQLAPL PRRRLRETLD RYENVKEFFW VQEEPANQGA WPRFGLELPE LLPDKLAGIK
RISRRAMSAP SSGSSKVHAV EQQEILDEAF G
