ID   A9CHK1_AGRFC            Unreviewed;       998 AA.
AC   A9CHK1;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
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:AAK88357.2};
GN   OrderedLocusNames=Atu2636 {ECO:0000313|EMBL:AAK88357.2};
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK88357.2, ECO:0000313|Proteomes:UP000000813};
RN   [1] {ECO:0000313|EMBL:AAK88357.2, ECO:0000313|Proteomes:UP000000813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2] {ECO:0000313|EMBL:AAK88357.2, ECO:0000313|Proteomes:UP000000813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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; AE007869; AAK88357.2; -; Genomic_DNA.
DR   RefSeq; NP_355572.2; NC_003062.2.
DR   RefSeq; WP_010972453.1; NC_003062.2.
DR   AlphaFoldDB; A9CHK1; -.
DR   STRING; 176299.Atu2636; -.
DR   EnsemblBacteria; AAK88357; AAK88357; Atu2636.
DR   GeneID; 66222823; -.
DR   KEGG; atu:Atu2636; -.
DR   PATRIC; fig|176299.10.peg.2639; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   PhylomeDB; A9CHK1; -.
DR   Proteomes; UP000000813; Chromosome circular.
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   Reference proteome {ECO:0000313|Proteomes:UP000000813};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          644..837
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   998 AA;  112240 MW;  0EF4EA95EBF7970E CRC64;
     MARQEANEQF QITSFLDGAN AAYIEQLYAR YEEDPSSVSP EWQSFFKALS DNPEDVKKAA
     KGASWKRANW PIPANGELVS ALDGNWATVE KAIEKKVQAK AEAKSADTGK PVSEAEVLQA
     TRDSVRAIMM IRAYRMRGHL HAKLDPLGIA SAVEDYNELS PKSYGFEESD YDRKIFIDNV
     LGLEYATVRE MVEILERTYC STLGVEFMHM SNPEEKGWIQ ERIEGPDKGV DFTPEGKKAI
     LSKLVEAEGY EQFLDVRFKG TKRFGLDGGE SLIPALEQII KRGGQDGLEE VVLGMAHRGR
     LNVLTNVMGK PHRAVFHEFK GGSFKPDDVE GSGDVKYHLG ASSDREFDGN KVHLSLTANP
     SHLEIVNPVV MGKARAKQDQ LAKTWDGDII PLSERAKVLP LLLHGDAAFA GQGVVAEILG
     LSGLRGHRVA GTMHFIINNQ IGFTTNPAFS RSSPYPSDVA KMIEAPIFHV NGDDPEAVVY
     AAKVATEYRM KFHKPVVIDM FCYRRFGHNE GDEPAFTQPK MYKVIRGHKT VARIYADRLI
     AEGLITEGDF EKVKADWRAH LEQEFEAGQS YKPNKADWLD GQWSGLRAAD NADEQRRGKT
     GVPMKQLKEI GKKLSTIPEG FTAHRTIQRF MENRSQMIET GEGIDWAMAE ALAFGSLVVD
     GHKIRLSGQD CERGTFSQRH SVLYDQETEE RYIPLANLAP TQARYEVINS MLSEEAVLGF
     EYGYSLARPN ALTLWEAQFG DFANGAQVVF DQFISSGERK WLRMSGLVCL LPHGYEGQGP
     EHSSARLERW LQMCAEDNMQ VANVTTPANY FHILRRQMKR DFRKPLILMT PKSLLRHKRA
     TSSLAELAGE SSFHRLLWDD AEVIKDGPIK LQKDAKIRRV VMCTGKVYYD LLEEREKRGI
     DDVYLLRVEQ LYPFPAKALI NELSRFRHAE MVWCQEEPKN MGSWSFIDPY LEWVLAHIDA
     KYQKVRYTGR PAAASPATGL MSKHLAQLAA FLEDALGE
//