ID   KGD_MYCSK               Reviewed;        1269 AA.
AC   A1UK81;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=2-oxoglutarate decarboxylase;
DE            EC=4.1.1.71;
DE   AltName: Full=Alpha-ketoglutarate decarboxylase;
DE   AltName: Full=2-oxoglutarate carboxy-lyase;
GN   Name=kgd; OrderedLocusNames=Mkms_4047;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Miller C.D., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes an oxidative decarboxylation from five-carbon
CC       2-oxoglutarate (alpha-ketoglutarate) to four-carbon succinate
CC       semialdehyde (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate = succinate semialdehyde +
CC       CO(2).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
CC       subfamily.
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DR   EMBL; CP000518; ABL93239.1; -; Genomic_DNA.
DR   RefSeq; YP_940029.1; -.
DR   GeneID; 4611987; -.
DR   GenomeReviews; CP000518_GR; Mkms_4047.
DR   KEGG; mkm:Mkms_4047; -.
DR   OMA; A1UK81; EGDEPAF.
DR   GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IEA:EC.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:InterPro.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR005475; Transketolase_central-reg.
DR   PANTHER; PTHR23152; 2oxoglutarate_DH_E1; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   ProDom; PD001115; 2Oxoacid_dh; 1.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Complete proteome; Decarboxylase; Lyase; Magnesium;
KW   Thiamine pyrophosphate; Tricarboxylic acid cycle.
FT   CHAIN         1   1269       2-oxoglutarate decarboxylase.
FT                                /FTId=PRO_0000310720.
FT   COILED      824    855       Potential.
SQ   SEQUENCE   1269 AA;  140119 MW;  F6F4221B80E76B83 CRC64;
     MSSSPSPFGQ NEWLVEEMYR KFREDPSSVD PSWHEFLVDY NPEPTTDSSA SENGQQTRTA
     APKAPPEPAP APAPKTPDSK TPDSKSQAPK QDSKPQESKP QAKAKPAESK SSTKPADAKS
     EKSGKSGTNG AAKPAAQPAD DSDQNQVLRG AAAAVAKNMS ASLDVPTATS VRAIPAKLMI
     DNRVVINNHL KRTRGGKISF THLIGYAIVA AVKKFPNMNR HFAEVDGKPN AVTPAHTNLG
     LAIDLQGKDG NRQLVVAAIK KADTMRFGQF IAAYEDIVRR ARDGKLTAED FSGVTISLTN
     PGTIGTVHSV PRLMRGQGAI IGVGAMEYPA EFQGASEERI ADLGIGKLIT LTSTYDHRII
     QGAESGDFLR TVHQLLLSDD FFDEIFRELG IPYEPVRWRT DNPDSIEDKN ARVIELIAAY
     RNRGHLMADI DPLRLDSNRF RSHPDLDVLT HGLTLWDLDR EFKVNGFAGA ERKKLRDVLA
     VLRDAYCRHI GVEYTHILEP EQQQWLQERI EGKHEKPTVA QQKYILSRLN AAEAFETFLQ
     TKYVGQKRFS LEGAETVIPA MDAVIDQCAE HALDEVVIGM PHRGRLNVLA NIVGKPYSQI
     FSEFEGNLNP SQAHGSGDVK YHLGSSGTYL QMFGDNDITV SLTANPSHLE AVDPVMEGLV
     RAKQDLLDKG DTEDGYTVVP LMLHGDAAFA GQGVVAETLN LALLRGYRTG GTIHLIVNNQ
     IGFTTSPAAA KSSEYCTDVA KMIGAPIFHV NGDDPEAAVW VSRLAVDFRQ KFKKDVVIDL
     LCYRRRGHNE GDDPSMTQPS MYDVIDTKRG VRKSYTEALI GRGDISMKEA EDALRDYQGQ
     LEQVFNEVRE LEKHEIEPSE SVEADQQIPA KLATAVDKSL LARIGDAHLA VPEGFTVHPR
     VKPVLEKRRE MAYEGKVDWA FAELLALGTM ISEGKLVRLS GQDTRRGTFT QRHSVVIDRK
     TGKEFTPLQL LATDSDGNPT GGKFLVYDSP LSEFAAVGFE YGYSVGNPDA MVLWEAQFGD
     FINGAQSIID EFISSGEAKW GQLSDVVLLL PHGHEGQGPD HTSGRIERFL QLWAEGSMTI
     ALPSTPANYF HLLRRHSLDG IQRPLIVFTP KSMLRNKAAV SDIRDFTEQK FRSVLEEPTY
     TDGDGDRNKV TRILLTSGKI YYELVARKNK ESRDDVAIVR IEQLAPLPKR RLAETLDKYP
     NVEEKFWVQE EPANQGAWPT FGLTLPEMLP DHFTGIKRIS RRAMSAPSSG SSKVHAVEQQ
     EILDEAFAP
//