ID   Q4KFY9_PSEF5            Unreviewed;       943 AA.
AC   Q4KFY9;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:AAY91013.1};
GN   OrderedLocusNames=PFL_1718 {ECO:0000313|EMBL:AAY91013.1};
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY91013.1, ECO:0000313|Proteomes:UP000008540};
RN   [1] {ECO:0000313|EMBL:AAY91013.1, ECO:0000313|Proteomes:UP000008540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC   {ECO:0000313|Proteomes:UP000008540};
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000076; AAY91013.1; -; Genomic_DNA.
DR   RefSeq; WP_011060052.1; NC_004129.6.
DR   AlphaFoldDB; Q4KFY9; -.
DR   SMR; Q4KFY9; -.
DR   STRING; 220664.PFL_1718; -.
DR   GeneID; 57474738; -.
DR   KEGG; pfl:PFL_1718; -.
DR   PATRIC; fig|220664.5.peg.1757; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000008540; 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:AAY91013.1};
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   943 AA;  106564 MW;  D9C6009067A3FABE CRC64;
     MQESVMQRMW NSAYLSGSNA AYVEELYELY LHDPNAVPEE WRTYFQKLPT DGSTAIDVSH
     STIRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AQLDPLGLWQ
     RPAPADLSIN HYGLTNADLD TTFRAGDLFI GKEEASLREI HEALQQTYCR TIGAEFTHIT
     DSEQRQWFQQ RLESVRGRPT YSADIKSHLL ERVTAAEGLE KYLGTKYPGT KRFGLEGGES
     LIPMLDELIQ RSGSYGTKEV VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKKVELGSGD
     VKYHQGFSSN VMTTGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDQ TGDKVLPISI
     HGDAAFAGQG VVMETFQMSQ TRGFRTGGTV HIVINNQVGF TISNPLDSRS TEYATDVAKM
     IQAPILHVNG DDPEAVLFVT QLAIDYRMQY KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY
     QQIAKQRTTR ELYADRLTQG GVLDAERVQA KVDEYRNALD NGLHVVKSLV KEPNKELFVD
     WRPYLGHTWT ARHDTTFDLK TLQELSAKLL ELPEGFVVQR QVAKIYEDRQ KMQAGGLPIN
     WGYAETMAYA TLAFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDAGTYIPL QHLYEGQPRF
     DLYDSFLSEE AVLAFEYGYS TTTPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAQIYHLLR RQVIRPLRKP
     LVVLTPKSLL RHKLAISTLE DLAEGSFQTV IPEIDAQDPK DVGRIILCSG KVYYDLLEKR
     RAEGRDDIAI VRIEQLYPFP EDDLIEVLAP YKNVKHIVWC QEEPMNQGAW YCSQHHMRRI
     ISGHNKSLVL EYAGRDASAA PACGYASMHA EQQEKLLQDA FTV
//