ID   A0A1W9HA20_9PROT        Unreviewed;       933 AA.
AC   A0A1W9HA20;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:OQW44111.1};
GN   Name=sucA {ECO:0000313|EMBL:OQW44111.1};
GN   ORFNames=A4S16_04135 {ECO:0000313|EMBL:OQW44111.1};
OS   Proteobacteria bacterium SG_bin6.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1827383 {ECO:0000313|EMBL:OQW44111.1, ECO:0000313|Proteomes:UP000192863};
RN   [1] {ECO:0000313|EMBL:OQW44111.1, ECO:0000313|Proteomes:UP000192863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG_bin6 {ECO:0000313|EMBL:OQW44111.1};
RX   PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA   Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT   "Comammox in drinking water systems.";
RL   Water Res. 116:332-341(2017).
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   -!- 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:OQW44111.1}.
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DR   EMBL; LWDJ01000049; OQW44111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9HA20; -.
DR   Proteomes; UP000192863; Unassembled WGS sequence.
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; 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; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          578..769
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          16..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  103236 MW;  D80F770084111F3B CRC64;
     MEMDSSFEPE YRPSWARAGW PIADTDERTA ALDPTQMAPA PKPDRGAKPA PAPAGGVDVP
     RASEDSIRAM MLIRTYRVRG HLAAKLDPLG IAKQELPADL TPEFHGFSGA DLDRPIYLGG
     ALGLQTATVR ELVDILRANY CGNVGLEYMH IADVEERRFL QDRMEGRDKA IEFTPNGKRA
     ILNKVIEAEQ WERFLGKKYV GTKRFGLDGG ESMIPALESI IKYGGQYGVR EIVYGMAHRG
     RLNVLANVMA KPLRVIFHEF GGGSQNPDDV GGSGDVKYHL GTSTDREFDG ISVHMSLVAN
     PSHLEAADPV VLGKTRAIQT IAGDLDEHAA SLPVLIHGDA AFAGQGIVWE CFGFSGLNGY
     NTGGCIHFVI NNQIGFTTSP QFARSSPYPS DVAKGVQAPI FHVNGDDPEA VTFACKMAIE
     YRQRFHRDVV IDMWCYRRFG HNEGDEPSFT QPLMYDRIRK HPPVSEVYGQ KLIAQGVVDQ
     AWIDETVKQF TLLLEGEFEA GQSYKPNKAD WFAGRWSGLH APADPETARR NIETGIDTKL
     FDAIGRVLTT VPDSVTIHKT LARVIDAKRA MFQTGEGFDW ATGEALAFGS LLHEGYGVRL
     SGQDSGRGTF SQRHAVWVDQ RDEHKFIPLG TIDQGRFEVL DSPLSEYGVL GFEYGYALAD
     PKTLVLWEAQ FGDFMNGAQI MIDQFIAAGE AKWLRANGLV MLLPHGYEGQ GPEHSSARPE
     RFLQLCAQDN MQVANCTTPA NYFHLLRRQM HRNFRKPLIV FTPKSLLRHK MAVSSAADFQ
     GESHFRRILS DPRAPADEAV KRLVLCTGKV AYDLIEARDA AGDAETAIVR IEQLYPFPGE
     PLAVRLKRMV NLEEVVWAQE EPKNNGAWFF VEPFIEECLA EAGVGPKRAR YAGRAAAASP
     ATGLAKRHQL EQGALVADAL GHSVREEIRR MQH
//