ID A0A094INV6_9GAMM Unreviewed; 738 AA.
AC A0A094INV6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:KFZ29335.1};
GN ORFNames=IDAT_02945 {ECO:0000313|EMBL:KFZ29335.1};
OS Pseudidiomarina atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ29335.1, ECO:0000313|Proteomes:UP000053718};
RN [1] {ECO:0000313|EMBL:KFZ29335.1, ECO:0000313|Proteomes:UP000053718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ29335.1,
RC ECO:0000313|Proteomes:UP000053718};
RA Du J., Lai Q., Shao Z.;
RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL Submitted (JUN-2014) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ29335.1}.
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; JPIN01000002; KFZ29335.1; -; Genomic_DNA.
DR RefSeq; WP_034730351.1; NZ_JPIN01000002.1.
DR AlphaFoldDB; A0A094INV6; -.
DR STRING; 1517416.IDAT_02945; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000053718; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 395..576
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 738 AA; 81149 MW; E8D7A7E2ABA537C7 CRC64;
MAAAMHPWLV EFIQRIERED LPRAHAAGGI LSDAELVELF DSQLASRLLD LQSRLMQAAG
QSFYTIGSSG HEANAAVAKA LRVTDPAFLH YRSGAFFLQR AKQKPGSTPL YDMLLSFAAS
SEDPISGGRH KVFGSLDLHV PPQTSTIASH VPKAMGTAFA IGLSKRLQQQ GTWPHDAIAV
CSFGDASANH STALGAINSA SWAAYQQIPM PLLLVCEDNG LGISTHTPQG WIQQQLSQRP
AVKYFFADGS NVAETYLVAQ QAADYVRQKR KPAILHLRTI RLFGHAGADA EVAYRTKQEI
ARDAERDVLL FTCAALIQRD LFSYEQLAEH IRKQAQRIAR LAGQAQQRPK LTAATQVMQS
IVPPARDESV VPPALTENQR EQLFRFDKHN VGKRQHLAKL LNWSLHDLMA QYDNIVMCGE
DIAKKGGVYH VTQHLMEAFG PNRVLNTVLD EQSILGLAIG MAQQGMIAMP EIQFLAYVHN
AEDQIRGEAA TLSFFSDGQY TNPMVIRIAG LAYQKGFGGH FHNDNSFAVF RDIPGVIVLC
PSNGYDGALL MRQAVRLAAV EQRVVIMLEP IALYMARDLH EEGDGGWLCD YPTPDVPVPA
LGEPAVYGDG DELAIVSYGN GYYLSRQAEA KLRAAGHKVR VVDIRCLVPL HVDAIVQSLG
DCKQVLIVDE CRRRGSLSEE LMTCLYEDYP ERFKVRRITA EDSFIPLGKA AYTVLPSTAG
IVEVASEMLA KRKQGAQA
//
