ID B1KGK0_SHEWM Unreviewed; 747 AA.
AC B1KGK0;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Transketolase central region {ECO:0000313|EMBL:ACA85328.1};
GN OrderedLocusNames=Swoo_1035 {ECO:0000313|EMBL:ACA85328.1};
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA85328.1, ECO:0000313|Proteomes:UP000002168};
RN [1] {ECO:0000313|EMBL:ACA85328.1, ECO:0000313|Proteomes:UP000002168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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};
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DR EMBL; CP000961; ACA85328.1; -; Genomic_DNA.
DR AlphaFoldDB; B1KGK0; -.
DR STRING; 392500.Swoo_1035; -.
DR KEGG; swd:Swoo_1035; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_6; -.
DR Proteomes; UP000002168; Chromosome.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002168};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 398..579
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 747 AA; 82256 MW; 3464A8CE90E9CF2C CRC64;
MEDRAVALDR SFIERVNKQD FSDIGEGWDH RKLGLSDSDF IGMFESQLKS RLLDLESRKM
RARNQGFYTI GSSGHEGNAA YGLTFRPTDM AFLHYRSGAF MIERSRQLSG ETILYDMLLS
FAASSDDPTS GGRHKVLGSK RLNIPPQTST IASHLPKAVG AALSIPLTQR LELASEMPSD
SVVLCNFGDA SANHASAQSA INSACWAAYQ QVPLPLVFIC EDNGIGISTR TPKGWIAASF
SQRASLKYFY CDGRDILDTY KVSREAADYA RVHRKPVFLH VRTVRLMGHA GSDAEIAYMK
KEHIFENEAQ DPLIVTAQQL IEARLMNSKQ IVALYESMKL RVEAIAKMAV TRPKLQTIEQ
AMASIVPQKR NVSDKPCLDE LSRGELFKAD KLALSKPLHM GKLLNLALTE LMARLDNIVV
CGEDVGKKGG VYHVTSRLVE RFGPNRVINT LLDETSILGL GIGMAHNGIL PIPEIQFLAY
VHNAEDQIRG EAATLPFFSD GQFTNPMVIR IAGLGYQKGF GGHFHNDNSF AVFRDIPGLI
IACPSNGADA VAMLRESVRL AHEEQRVVIF LEPIALYMTK DLHETGDGLW ASDYIPEQDS
TPLALGDITT EGRGDELCII SYANGYYLSR QAQKVLMETG LKVRVIDIRW LAPLNIDGIV
AQAKECKHIL IVDECRKTGS ISEALMTGFA EALREACPPI ARLTADDCFI PLADAATLPL
PSKESIIEAA MNLIGKELNQ ALLKEAL
//
