ID A0A0R0CF97_9GAMM Unreviewed; 756 AA.
AC A0A0R0CF97;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:KRG67686.1};
GN ORFNames=ABB27_08910 {ECO:0000313|EMBL:KRG67686.1};
OS Stenotrophomonas terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405446 {ECO:0000313|EMBL:KRG67686.1, ECO:0000313|Proteomes:UP000051863};
RN [1] {ECO:0000313|EMBL:KRG67686.1, ECO:0000313|Proteomes:UP000051863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18941 {ECO:0000313|EMBL:KRG67686.1,
RC ECO:0000313|Proteomes:UP000051863};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG67686.1}.
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; LDJJ01000028; KRG67686.1; -; Genomic_DNA.
DR RefSeq; WP_057628341.1; NZ_LDJJ01000028.1.
DR AlphaFoldDB; A0A0R0CF97; -.
DR PATRIC; fig|405446.3.peg.1233; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000051863; 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 421..602
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 756 AA; 81809 MW; 801E80997BB44F7F CRC64;
MFARVPNPIP ARMKGLNRAE ICDTNFIEFV SALAPGPVQG PQPAAPILPG SALDAQGFRE
LFESQLVSRH LDLMARVLRV QNKVFYTIGS SGHEGNAMVA RAARHTDPAF LHYRSGGFMA
ERFRKLPGMD PVMDSALSFA ASKDDPASGG RHKVWGSKPL WVLPQTSTIA SHLPKALGTA
MAIEAGKRLG QGLPIPDDSI TICSFGDASA NHATAQTAFN AAAWSSFQKL PAPVLFVCED
NGIGISVKTP AGWIGESFRQ RPGLDYFQAD GLDLATGYAD VQRAVEHCRR TRRPTFLHLR
TTRLMGHAGT DFEIEWRALE ELCAVEAGDP LLRSAQIAIE SGLMDKAEVL VLYEQTRQRC
FAAAEDADQR PRLTELQDVI APLAPYTPDK VQAEATRADH AERRLQVFGS EAGLPENQPA
RHLAVQINQA LHDLFAKYPE TLLFGEDVAQ KGGVYTVTKG LQKAFGPRRV FNTLLDETMI
LGMAQGFANM GMLPLPEIQY LAYLHNAIDQ VRGEACSLQF FSNDQYRNPM LIRIAGLGYQ
KGFGGHFHND NSITAIRDIP GLVVGCPSRG DDAAAMLRTL AALAKVDGRV SVFLEPIALY
MTKDLYAPGD GQWLFPYPAP DQALVLGEGR VYGEGNDDLL IISYGNGVPM ALRAAKTIEQ
QHGWKVRVVD LRWLVPLNAS YIAAQAKGAK RIIVLDEGRH SAGVGEGVIT ALVEAGLAQV
PLRRVTGVDT YTPLAGAALL VLPGDADVVA AAAELA
//
