ID   A0A0Q8EUP6_9GAMM        Unreviewed;       754 AA.
AC   A0A0Q8EUP6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=MFS transporter {ECO:0000313|EMBL:KRA51086.1};
GN   ORFNames=ASD77_15775 {ECO:0000313|EMBL:KRA51086.1};
OS   Pseudoxanthomonas sp. Root65.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA51086.1, ECO:0000313|Proteomes:UP000051430};
RN   [1] {ECO:0000313|EMBL:KRA51086.1, ECO:0000313|Proteomes:UP000051430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root65 {ECO:0000313|EMBL:KRA51086.1,
RC   ECO:0000313|Proteomes:UP000051430};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA51086.1, ECO:0000313|Proteomes:UP000051430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root65 {ECO:0000313|EMBL:KRA51086.1,
RC   ECO:0000313|Proteomes:UP000051430};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRA51086.1}.
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DR   EMBL; LMHA01000003; KRA51086.1; -; Genomic_DNA.
DR   RefSeq; WP_055944144.1; NZ_LMHA01000003.1.
DR   AlphaFoldDB; A0A0Q8EUP6; -.
DR   STRING; 1736576.ASD77_15775; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000051430; 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   Reference proteome {ECO:0000313|Proteomes:UP000051430};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          419..600
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   754 AA;  82192 MW;  080622EC9E0C9DB6 CRC64;
     MTAHHPIPAR MKGLNRAEIC DQNFIEFVKA WSGRVGAKPA AGDAVLPGSR LDAEGFIELL
     ESQLISRHLD LMARVLRVQN KVFYTIGSSG HEGNAMVARL TRHTDPAFLH YRSGGFMAER
     FRKLPGMDPV MDSALSFAAS ADDPASGGRH KVWGSKPLWV LPQTSTIASH LPKALGTAVA
     IEQARRIGHA LPIPDDSIAI CSFGDASSNH ASAQTAFNAA AWTAYQKLPA PVLFVCEDNG
     IGISVKTPEG WIGRNFRDRK DLDYFHADGL DLATGYGQVQ AAVEHCRRTR RPTFLHLRTT
     RIMGHAGTDF EIEWRPLEEL CAVEATDPLL RSAAIALESG LLSKDALLDL YEATRRRCFA
     AAEDADRRPR ITTLEHVMAP VAPYTPDAVA KEAARTAPHE KRVAAFGSED KLPEKLPPRH
     LAIQINNALH DLLCKYPETL LFGEDVAQKG GVYTVTKGLQ KAFKGTRVFN TLLDETMILG
     LAQGYANLGM LPIPEIQYLA YFHNACDQIR GEAASLQFFS NNQYRNPMVV RIAGLGYQRG
     FGGHFHNDNS ITALRDIPGL VVGCPSRGDD AAMMLRTLAA LAKVDGRVSI FLEPIALYMT
     KDLHEAGDGQ WLFPYPAQDA AMPLGEGRLY NEDADDLVIF TYGNGVPMSL RAARGIENKH
     GWKVRVVDLR WLVPLNATFI AAQAKTARRI LVVDEGRHAA GVGEGVITAI AEAGYAARPF
     QRVVGADTYT PLASAAFLVL PGDEDIVAAA DRLA
//