ID A0A127W0N0_SPOPS Unreviewed; 936 AA.
AC A0A127W0N0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AZE41_12150 {ECO:0000313|EMBL:AMQ06619.1};
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ06619.1, ECO:0000313|Proteomes:UP000071057};
RN [1] {ECO:0000313|EMBL:AMQ06619.1, ECO:0000313|Proteomes:UP000071057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ06619.1,
RC ECO:0000313|Proteomes:UP000071057};
RA Yan W.;
RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014616; AMQ06619.1; -; Genomic_DNA.
DR RefSeq; WP_067209738.1; NZ_CP014616.1.
DR AlphaFoldDB; A0A127W0N0; -.
DR STRING; 1476.AZE41_12150; -.
DR KEGG; spsy:AZE41_12150; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000071057; Chromosome.
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; 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; 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 591..787
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 910..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 104615 MW; 1A82869EDBECB9F2 CRC64;
MSNNADAHRS PYAAFSGPNL GYIMEMYELF KTSPESIDAE LAEMFSRFGA PTISNTEQDK
AVGAVAPGDF GKVFSAYQLQ TAIRTYGHLA ADIYPLSDRP KDSTRLELST YGLTESDLQA
MPASLFFKNV PASVEDGLEA VNYLKSLYTG KIAYEFDHVI DEEERNWIQS KIENGNVSAT
LSVDEKKALL ERLTKIEGFE KFIHRTFVGA KRFSIEGLDT LVVFLDELVR LSEEQKMKKV
LIGMAHRGRL NVLTHILNKP YETMFAQFAG VPEEPFLPTD GSLETTRGWF GDVKYHMGAL
YKGQSGMQRF LAYNPSHLEV VNPVVTGQTR AAQENTDNPG IPVLETDAAY AVLIHGDAAF
PGQGIVPESF NYSRVRGFKT GGSIHVIANN MIGFTTEYYD SRSTHYSSDP AKGYEVPVLH
VNADSPESVI AAASFAFEYR QKFSKDILID LLGYRRYGHN EMDEPLVTNP VMYHSIHEHP
TVRALYGSEL ASENILTEED VTKLDASVFA TMQAAYDKVK EHTSEKTLIS NATPEEVLAG
YPRDLETGTD EANLRRINEE LLIYPENFNV FGKLGKILKR REDPFNGKGK IDWAHAETLA
FGAILQDGNP IRMTGQDVQR GTFAHRHVVL HDEKTGDELV PLHHISGSKA SFVAYNSPLT
EAAIVGYEFG YNLEDQKVLS IWEAQYGDFS NMAQVMFDQF VSSSYSKWGQ QSGLVLLLPH
AYEGQGPEHS SARLERYLQL CAENNWTVAN LSSAANYFHI LRRQAKMLGD KSMRPLVIVS
PKSLLRHPLV GADVNDLTEG HFQTVLEQPG TGKNTDKVEK ILFASGKVAI DLAERVKDGK
GFDHLHIVRV EQLYPFPADK ISDIISRYPN AKELVWVQEE PKNMGSWHFA NSYIREVADG
KKVSYVGRIH RSSPSEGDGE SHKIEQNRIL DEALKK
//
