ID A0A0M2VIX1_9GAMM Unreviewed; 753 AA.
AC A0A0M2VIX1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:KKO49013.1};
GN ORFNames=VT06_08465 {ECO:0000313|EMBL:KKO49013.1};
OS Arsukibacterium sp. MJ3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO49013.1, ECO:0000313|Proteomes:UP000034895};
RN [1] {ECO:0000313|EMBL:KKO49013.1, ECO:0000313|Proteomes:UP000034895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO49013.1,
RC ECO:0000313|Proteomes:UP000034895};
RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA Stougaard P., Glaring M.A.;
RT "Draft genome sequences of two protease-producing strains of
RT Arsukibacterium isolated from two cold and alkaline environments.";
RL Submitted (MAR-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:KKO49013.1}.
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DR EMBL; LAHP01000009; KKO49013.1; -; Genomic_DNA.
DR RefSeq; WP_046553864.1; NZ_LAHP01000009.1.
DR AlphaFoldDB; A0A0M2VIX1; -.
DR STRING; 1632859.VT06_08465; -.
DR PATRIC; fig|1632859.4.peg.1758; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000034895; 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 CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 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:UP000034895};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 394..575
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 753 AA; 81539 MW; 99C52C6915499995 CRC64;
MAEPFHPWLE SFLQRINSNN LPSVSSLQQS LSDSVLYRLW HSQLSSRLLD LQSRLLQAKG
QSFYTIGSAG HEGNAAVAAA LRLTDPAFLH YRSGAFFIER SKQLPGSTPL YDMLLSFCAS
SDDPISGGRH KVLGSLALNI PPQTSTIASQ LPKAVGAAFA IDLSKRLGQA GSWPHDAIVM
CSFGDASANH STAQGAINAA CWAAYQHVPL PLLFVCEDNG LGISTPTPQG WIEQSLADRP
ELRYFAADGR DLAQSYTAAR NAAQYVRRKR QPALLHLSTV RLFGHAGADT EAAYRSKIQV
AAELELDPLL ASTACVLARG IVSRQQLQQA ITELASQISR VAQVASSRPK LHSAAAIMAA
IAPVKPAMPA PPLPLPAIRS ALFEFDKHNM AKPQHLAKLL NWTLHDLFAQ YHNVVLFGED
VGKKGGVYGV SQHLVHAFGA NRVINTLLDE QSILGMAIGL AQQGLLPIAE IQFLAYVHNA
EDQIRGEAAT LPFFSNGQYH NAMVIRIAGL AYQRGFGGHF HNDNSFAVFR DIPGIIVLCP
SNGADAALLL RQAVQLAAEQ KRLVIFLEPI ALYMTRDLLS AGDGGWLCDY PTPDTPLPAL
GEPAVFNQGP AYEQNRAARP QLAIISYGNG YYLSRQAAAE LQSAGYNLRL LDIRCVVPLH
IDAIVAALDG CQQVLIVDEC RRRGSLSEEL FTALHEARPG WYQLSRITAM DSFIPLGTAA
YAVLPSKQQI MDKVLQLIEQ TPKPSAATTG APL
//
