ID F5Z7K0_ALTNA Unreviewed; 939 AA.
AC F5Z7K0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=sucA {ECO:0000313|EMBL:AEF03043.1};
GN OrderedLocusNames=ambt_07575 {ECO:0000313|EMBL:AEF03043.1};
OS Alteromonas naphthalenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF03043.1, ECO:0000313|Proteomes:UP000000683};
RN [1] {ECO:0000313|EMBL:AEF03043.1, ECO:0000313|Proteomes:UP000000683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC {ECO:0000313|Proteomes:UP000000683};
RX PubMed=21705606; DOI=10.1128/JB.05252-11;
RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA Oh T.K., Kim J.F.;
RT "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT bacterium Alteromonas sp. strain SN2.";
RL J. Bacteriol. 193:4292-4293(2011).
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|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP002339; AEF03043.1; -; Genomic_DNA.
DR RefSeq; WP_013783983.1; NC_015554.1.
DR AlphaFoldDB; F5Z7K0; -.
DR KEGG; alt:ambt_07575; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000000683; Chromosome.
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: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 InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEF03043.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 597..790
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 939 AA; 105041 MW; 4286F3A53E2215F3 CRC64;
MQESVMKAWW DSSHMAGANA AYVEELYESY MEDPQSVSDT WRQIFDSLPK VEGVELETNH
TSVKDQFRKL AALGPTARMS SAPVEGTPVS DDRQVKVLQL INAFRFRGHQ HANLDPLGLW
KQERVRDLEL SHHNLSDKDF DSVFNVGSFA IGKDSMSLGE LFKSLNRTYC GSIGAEYMHI
TDTDQKRWLQ QKIESVQAKP EFSKDEKLTL LKGLTAADGM EKYLGSKFPG AKRFSLEGGD
ALVPMLKNLI TNAGAAGTKE VVIGMAHRGR LNVLVNVLGK NPSVLFDEFA GKHDDSLGAG
DVKYHAGFSS DFATPGGNVH LALAFNPSHL EIVNPVVMGS VRARLERRND DTNTVLPITI
HGDSAIAGQG VVQETFNMSQ TRGFAVGGTV RIVVNNQVGF TTSKTEDTRS TQYCTDIAKM
VQAPIFHVNS DDPEAVAFVT QLALEYRNKF KRDVVIDLVC YRRHGHNEAD EPNATQPLMY
QKVKKHPVPR AIYADQLIAE GVIEQRDADR YLEEYRAALD HGACVVEEWR PMTKHSVDWS
PYLGHDWDTP YDGAISVEKL QALGEALTSF PEGHKLQSRV NKLYQDRKAM VSGEKKLDWG
MAENLAYASL VDAGEDIRMT GQDSGRGTFF HRHAVLHNQA DGSTYMPLQN IREGQGEIEI
YDSVLSEEAV MAFEYGYATA EPECLTIWEA QFGDFANGAQ VVFDQFLSSG EAKWGRLCGL
TMLLPHGYEG QGPEHSSARL ERFLQMCADH NWQVCVPSTP AQVFNMLRRQ VVRPMRKPLI
VMSPKSLLRH PLATSSLEEL AEGKFHNVIS EIDDINPKDV KRVVMCSGKV YYDLLDQRRK
NEQTDVAIVR LEQLYPFPQE ECAKVVAQYS HVTDWVWCQE EPQNQGAWYC SQHHFWQAIP
DGAKLTYAGR EASSSPAVGY VSVHNQQQKA LVEDALTIK
//
