ID A0A0Q9XPC1_9STAP Unreviewed; 933 AA.
AC A0A0Q9XPC1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|HAMAP-Rule:MF_01169};
DE EC=1.2.4.2 {ECO:0000256|HAMAP-Rule:MF_01169};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01169};
GN Name=odhA {ECO:0000256|HAMAP-Rule:MF_01169};
GN ORFNames=ACA31_04585 {ECO:0000313|EMBL:KRG10160.1};
OS Staphylococcus sp. NAM3COL9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1667172 {ECO:0000313|EMBL:KRG10160.1, ECO:0000313|Proteomes:UP000051126};
RN [1] {ECO:0000313|EMBL:KRG10160.1, ECO:0000313|Proteomes:UP000051126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA309 {ECO:0000313|EMBL:KRG10160.1,
RC ECO:0000313|Proteomes:UP000051126};
RA Gaiero J., Nicol R., Habash M.;
RT "Genome sequencing project of Staphylococcus sp. NA309.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|HAMAP-Rule:MF_01169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|HAMAP-Rule:MF_01169};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|HAMAP-
CC Rule:MF_01169}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_01169}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG10160.1}.
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DR EMBL; LGPC01000011; KRG10160.1; -; Genomic_DNA.
DR RefSeq; WP_057512186.1; NZ_LGPC01000011.1.
DR AlphaFoldDB; A0A0Q9XPC1; -.
DR PATRIC; fig|1667172.3.peg.946; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000051126; Unassembled WGS sequence.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR HAMAP; MF_01169; SucA_OdhA; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
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 NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01169};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01169};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 590..786
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 933 AA; 105709 MW; D950A90F5842698A CRC64;
MSNERQVSEA PVNFGANLGY VLDLYDVYLN DPTSVPEDLQ VLFSTIKNGE ANIVTNTEGQ
SNVTKGDSTI KRVMRLIDNI RQYGHLLADI YPVNRPVREN VPKLNFEDFN LDKETLESIS
AGIVSEHFKD IYDNAYEAIV RMEKRYKGPI AFEYTHINNN RERVWLKRRI ETPYKATLND
NKKIELFKNL AHVEGFEKYL HKNFVGAKRF SIEGVDTLVP MLQQTLKLAS DEGIQNIQIG
MAHRGRLNVL THVLEKPYEM MISEFMHTDP MKFLPEDGSL KLTSGWSGDV KYHLGGVKTT
RSYGSEQRIS LANNPSHLEI VAPVVLGKTR ATQDNTDKPG AVTTEFEKSM PILIHGDAAY
PGQGINFEAM NLGSLDGYST GGTLHVITNN RIGFTTEPEE GRSTTYSSDV AKGYDVPIMH
VNADNVEATI EAIEIAMAFR KEFHKDVVID LVGYRRYGHN EMDEPSITNP LQYHEIRKHE
SVELLYGRQL VDENIITEDQ MNNIMDEVQK SLRASHDKID KNDKMDNPNM QKPDDLAEPI
QSEDTELSFE HLKEINDAML TYPSNFNVLK KLNKVLDKRR EPFEKEDGLV DWAQAEQLAF
ATITQNGNPI RLTGQDSERG TFSHRHAVLH DPETGEKYTP LHHVPNQKAT FEVRNSPLSE
AAVVGFEYGY NVQNKSCMTI WEAQYGDFSN MSQMIFDNFL FSSRAKWGER SALTLLLPHS
FEGQGPEHSS ARLERFLQLA GENNATIVNL SSSSNYFHLL RAQAATLGTE SMRPLVVMSP
KSLLRNKTVA DPISKFTTGK FEAILPEEHQ KDAVRKVILA SGKMFIDLKE YLAKNPNDSI
LIVAVERLYP FPVTEIEALL NELPNLENVA WVQEEPKNQG AWSFVYPCLK ELTTDRYDLS
YHGRIQRSAP AEGDGEIHKL VQNMILEQST KIN
//
