ID   G2IIR8_SPHSK            Unreviewed;       939 AA.
AC   G2IIR8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:BAK64748.1};
GN   ORFNames=SLG_00730 {ECO:0000313|EMBL:BAK64748.1};
OS   Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK64748.1, ECO:0000313|Proteomes:UP000001275};
RN   [1] {ECO:0000313|EMBL:BAK64748.1, ECO:0000313|Proteomes:UP000001275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275};
RX   PubMed=22207743; DOI=10.1128/JB.06254-11;
RA   Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA   Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA   Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA   Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT   lignin-derived biaryls and monoaryls.";
RL   J. Bacteriol. 194:534-535(2012).
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; AP012222; BAK64748.1; -; Genomic_DNA.
DR   RefSeq; WP_014074400.1; NC_015976.1.
DR   AlphaFoldDB; G2IIR8; -.
DR   STRING; 627192.SLG_00730; -.
DR   KEGG; ssy:SLG_00730; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000001275; 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; 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   ECO:0000313|EMBL:BAK64748.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001275};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          583..774
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   939 AA;  103977 MW;  2E137B32D0A8C032 CRC64;
     MGFENQDFTG QGEVEQGPSW ARKGWPLDTT DDLTAALDPT QMQLAVKAAS AKSGATLSEA
     DIAKAAGDSI RAMMLIRTYR VRGHLAANLD PLGLVQRDLP ADLTPEYHGF SGADLDRKVY
     IGGSLGLEWA TIREIVDILR ANYCGNVGLD YMHIADVEER RFLQERMEGK DKEIIFTENG
     KKAILAKVIQ AEQYEKFLGR KYVGTKRFGL DGGESMIPAL EAVIKYGGQL GVREIVYGMA
     HRGRLNVLAN VMAKGFRVIF HEFSGGTANP EDVGGSGDVK YHLGTSTDRE FDGINVHMSL
     VPNPSHLETV DPIVLGKVRA QQVFRDDIGP GQHKQVLPVL IHGDAAFAGQ GIVWECFGFS
     GVRGYNTGGC IHFVVNNQIG FTTSPQFARS SPYPSDVAKG VQAPILHVNG DDPEAVTFAC
     KLAIEYRQTF HRDIVIDMWC YRRFGHNEGD EPSFTQPQMY AQIKQHPPVS EVYAARLREE
     GVVDDAFIQA TADGFVALLE EEFEAAKTYK SNHADWFAGR WSGLHQPADI ETARKNVESA
     ISPKLFESLG RTLTTVPQDL NVHRTLRRIL DAKAEMFRTG EGFDWATGEA LAFGSLLSEG
     YGVRLSGQDS GRGTFSQRHA VWLDQETERK YIPLSTVPHG HFEVYDSPLS EYGVLGFEYG
     YAMADPKSLV LWEAQFGDFA NGAQIIVDQY IAAAEAKWLR ANGLVLLLPH GYEGQGPEHS
     SARVERYLQL CAEGNIQVAN CTTPANYFHI LRRQMLRPFR KPLILMTPKS LLRHKLAVSK
     AEDFMGDRHF QRILSDPNGS ADAQTRKLVL CTGKVAYDLL EARDAAGDKH TQIVRVEQLY
     PFPTEALSVR LKRLPALEEV VWCQEEPRNN GAWFFVEPFI EQALSDAGKG PMRARYAGRK
     PAASPATGLA RRHAAEQGAL VADALGHSVR TEIRRQKKA
//