ID   A1UQW1_BARBK            Unreviewed;       999 AA.
AC   A1UQW1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:ABM44563.1};
GN   OrderedLocusNames=BARBAKC583_0025 {ECO:0000313|EMBL:ABM44563.1};
OS   Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095 {ECO:0000313|EMBL:ABM44563.1, ECO:0000313|Proteomes:UP000000643};
RN   [1] {ECO:0000313|EMBL:ABM44563.1, ECO:0000313|Proteomes:UP000000643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583
RC   {ECO:0000313|Proteomes:UP000000643};
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) 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|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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|ARBA:ARBA00011301}.
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DR   EMBL; CP000524; ABM44563.1; -; Genomic_DNA.
DR   RefSeq; WP_005765715.1; NC_008783.1.
DR   AlphaFoldDB; A1UQW1; -.
DR   STRING; 360095.BARBAKC583_0025; -.
DR   GeneID; 72471600; -.
DR   KEGG; bbk:BARBAKC583_0025; -.
DR   PATRIC; fig|360095.6.peg.25; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000000643; 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:ABM44563.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000643};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          645..838
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   999 AA;  112844 MW;  C6AE57FD9C68C6C6 CRC64;
     MAKQHKINDV FAQTSFLYGG NANYIDQLYA EYEKNPDSVD LQWRAFFENL QDNKEDVLKN
     AEGASWQRNH WPLKESGELV SALDGDWSAL EKHLGDKLKE KAATGAAQKG ETPNQQDMAR
     AIRDSFNALM MIRAFRTRGH LLAQLDPLRL IKNPEECKEL SPEAYGFSPA DYERPIFIDN
     VLGLEYATIP QILEILKRTY CSTIGVEYMH IADPAQKAWI QERIEGSNKQ SAFTQEDKKT
     ILDKLIEAEG FEQFLDTKYK GTKRFGLDGG EALIPALEQV IKTGGNLGVQ EVVFGMAHRG
     RLNVLSQILA KSHRAIFYEF KGGSYKPDDV AGSGDVKYHL GASTDREFNG KKIHLSLLPN
     PSHLEIVDPV VIGKARAKQD QLVGSTRMDV IPLAERSKVM PVLIHGDAAF AGQGVLQETF
     GLSGLKGYHV AGSIHVIINN QIGFTTSPNF SRSSPYSSDV AKMIDAPVFH VNGDDPEAVV
     FVAKVATEFR QIFHKPVIID MVCYRRYGHN EGDEPSFTQP VMYKAIRNHQ TTVQIYSDRL
     ISEQLINSEE VEHKKKIWRD KLEVEFEAST SYKPNKADWL DGVWTGLKTA NHADEQRRGI
     TGIELKALIE IGRKLVEIPS DFHVHKTIQR FLSNRAKMFE TGEGIDWATA EALAFGSLCC
     EGIPVRLSGE DVERGTFSQR HSVLYDQENE ARYIPLNNLQ KGQAIYEVVN SMLSEEAVLG
     FEYGYSLASP LGLTLWEAQF GDFANGAQVI FDQFISSAEH KWLRMSGLVC LLPHGFEGQG
     PEHSSARLER YLQLCAEDNM QVAYCTTPAN YFHILRRQIK RDFRKPLILM TPKSLLRHRR
     AVSSLSDMGL QTNFHRLLLD DAECLRDSVI KLQKDSKIRR VVLCTGKVYY DLYEEREKRG
     IDDVYLLRIE QLYPFPAKTL VEVLSRFVKA EIVWCQEEPK NMGAWSFIEP YLEWVLVHIK
     AKYSRARYAG RPASASPATG LMSKHLEQLA AFLEDALGS
//