ID   A0A2Z3HVY3_9CAUL        Unreviewed;       952 AA.
AC   A0A2Z3HVY3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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:AWM78386.1};
GN   ORFNames=HYN04_11885 {ECO:0000313|EMBL:AWM78386.1};
OS   Phenylobacterium parvum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=2201350 {ECO:0000313|EMBL:AWM78386.1, ECO:0000313|Proteomes:UP000247763};
RN   [1] {ECO:0000313|Proteomes:UP000247763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYN0004 {ECO:0000313|Proteomes:UP000247763};
RA   Yi H., Baek C.;
RT   "Genome sequencing of Phenylobacterium sp. HYN0004.";
RL   Submitted (MAY-2018) 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; CP029479; AWM78386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z3HVY3; -.
DR   KEGG; phb:HYN04_11885; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000247763; 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:AWM78386.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247763};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          599..792
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   952 AA;  105711 MW;  5F8A25B6502DE693 CRC64;
     MADDAGRINE LLAETSFLYG GNAAFIEDLY ARWMKAPDSV EASWRSFFAS IHDRAGAAQP
     MAPPAWTARK APAAAGQDVR AATLDSLRAI MMIRAYRMRG HLRANLDPLG IAIPEGDASE
     LDPASYGFTE ADYDRPIFLD YVLGLETGTL REILAILKRT YCADIGVQYM HISDPAQKAW
     LQERIEGRDK EIVFTREGKI AILKKLIEAE GFERFLHKRF PGTKRFGLDG GEAMVPALEQ
     IIKRGGALGV RDIVIGMPHR GRLNVLAAVM GKPYRVIFHE FQGGSTLPTD VEGSGDVKYH
     MGASSDRAFD GNSVHLSLTA NPSHLEIVNP VVLGKARAKQ AFVLRETSDA GRNHVLPLLM
     HGDAAFAGQG VVAECFAISG TKGYRTGGCI HFIVNNQIGF TTAPKYSRSS PYPSDVALMV
     EAPIFHVNGD DPEATVYAVK VATEFRQKFG RDVVIDMFCY RRFGHNEGDD PTMTSPLMYA
     RIKDHPSTRE IYTRQLVAEG VVSEDDVSRW MGEFEAFLDA EFEAGKTYKA DKADWLDGKW
     AGLALPEGED RRGNTSVPLP RLKSLGAAIT AIPDGIDVHK NVRRVIEGRK SAIESGEGLD
     WATAEHLAFG SLLQDGFPVR LAGQDSVRGT FTQRHCGIID QTTEAQYTPL NNLGAGQAHF
     EVIDSPLSEE AVLGFEYGFS LADPKTLVLW EGQFGDFANG AQVVIDQFIS SGERKWLRMS
     GLVLLLPHGY EGQGPEHSSA RLERFLQLCA EDNMQVVNCT TPANYFHVLR RQMKREFRKP
     LVVMTPKSLL RHKKAVSLLA EMAEGSSFHR VLHDDAERGR HTALTLDPPE KIRRVVLCSG
     KVYYDLLEAR EEKGLTDIYL MRLEQFYPWP MKSLSTELSR FPNAELVWCQ EEPKNMGGWT
     FVDPWLELTL ERLKVKAKRA RYVGRPASAS TAAGQMSRHN RELQAFLTEA LA
//