ID A0A1S6HVV5_9GAMM Unreviewed; 747 AA.
AC A0A1S6HVV5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component {ECO:0000313|EMBL:AQS39707.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:AQS39707.1};
GN ORFNames=Sps_04622 {ECO:0000313|EMBL:AQS39707.1};
OS Shewanella psychrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225848 {ECO:0000313|EMBL:AQS39707.1, ECO:0000313|Proteomes:UP000189545};
RN [1] {ECO:0000313|EMBL:AQS39707.1, ECO:0000313|Proteomes:UP000189545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP2 {ECO:0000313|EMBL:AQS39707.1,
RC ECO:0000313|Proteomes:UP000189545};
RA Xu G., Jian H.;
RT "Complete genome sequence of Shewanella psychrophila WP2, a deep sea
RT bacterium isolated from west Pacific sediment.";
RL Submitted (MAR-2016) 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; CP014782; AQS39707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6HVV5; -.
DR STRING; 225848.Sps_04622; -.
DR KEGG; spsw:Sps_04622; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000189545; Chromosome.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:AQS39707.1};
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; 82549 MW; 58B03650AE860C53 CRC64;
MEDRALVLDR RFLERVQKLE FSDIGEGWNH QRIGLTDSDF IGLFESQLKS RLLDLESRKM
KGRNQGFYTI GSSGHEGNAA YGLAFRPTDM AFLHYRSCAF MLERGRQVPG ETLLYDILLS
FAASSDDPTS GGRHKVLGSK RLNIPPQTST IASHLPKAVG AALSIPLTDR LSLASNMPTD
SVVLCNFGDA SANHASAQSA INSACWAAYQ QVPMPLVFIC EDNGIGISTP TPKGWISANF
SQRPGLKYFC CDGRDILDCY KISKEAADFA RVHRKPVFLH VRAVRLMGHA GSDAEIAYMK
KQQIFDNESQ DPLLVSAQQL IEAGVMNSEQ IISLYLSLKA RIEAISRIAV TRPKLRDVNQ
AMKAIVPPKC RLESIPYLEE ERRSILLKAD KQSLIKPLHM GKMINLALTE LMARYSNIVV
CGEDVGKKGG VYHVTSRLVE RFSPNRVINT LLDETSILGL AIGMAHNGIL PIPEIQFLAY
VHNAEDQIRG EAATLPFFSD GQFTNPMVIR IAGLAYQKGF GGHFHNDNSF AVFRDIPGLI
IACPSNGHDA VEMLRECVRL AREEQRVVIF LEPIALYMTK DLHKKDDGLW SSHYLPEQEA
KPVALGEIAQ YGEGMDLCII SYANGYYLSR QAEKVLAATG LNVRVLDIRW LAPLNMQAII
NSAKECHHIL IVDECRKTGS ISEAIISGFH EALGNECPPL ARLTAEDCFI PLADAATLPL
PSRDSIVEAA LALIGKELNH QLLKEAL
//
