ID A0A014MIR0_9BURK Unreviewed; 1207 AA.
AC A0A014MIR0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:EXU81601.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:EXU81601.1};
GN ORFNames=AX13_07300 {ECO:0000313|EMBL:EXU81601.1};
OS Comamonas aquatica DA1877.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU81601.1, ECO:0000313|Proteomes:UP000020766};
RN [1] {ECO:0000313|EMBL:EXU81601.1, ECO:0000313|Proteomes:UP000020766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU81601.1,
RC ECO:0000313|Proteomes:UP000020766};
RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA Caudy A.A., Walhout A.J.;
RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT Gene Expression and Life History Traits.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:EXU81601.1}.
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DR EMBL; JBOK01000002; EXU81601.1; -; Genomic_DNA.
DR RefSeq; WP_043378538.1; NZ_JBOK01000002.1.
DR AlphaFoldDB; A0A014MIR0; -.
DR STRING; 225991.MA05_02305; -.
DR PATRIC; fig|1457173.3.peg.478; -.
DR Proteomes; UP000020766; Unassembled WGS sequence.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR046667; DUF6537.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EXU81601.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020766}.
FT DOMAIN 483..574
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 778..965
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 992..1190
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1207 AA; 132289 MW; B7DD02E07B123116 CRC64;
MNAPLDDVTR RALESITLDD KYTLERGRAF MSGVQALVRL PMLQRQRDAK HGLNTAGFIS
GYRGSPLGTY DQSLWAAKKH LEAQHIVFQP GVNEELAATA VWGTQQLDLY PQTKKYDGVF
GIWYGKGPGV DRCSDVFKHA NMAGTAQHGG VIAIAGDDHI SKSSTAAHQS DHIFKACGTP
VFFPSNVQDI LDMGLHAFAM SRFSGLWSGM KTIQEVVESS ASIAVDPDRV NIVLPEDFQM
PPGGLHIRWP DAPLEQEARL MDYKWYAALA YVRANKLNYN VVQGANDRFG LIASGKAYND
MRQALVDLGL DDAVCRQLGI RVHKVNVVWP LEASITRDFA QGLQEILVVE EKRQVIEYQL
KEELYNWRPD VRPNVLGKFD EQPGDDSGGE WSMPNPSQNW LLRPKADLTP AIIAQAIAKR
LKKLGVPADI EARMEQRLAV IAARERALAE LPAGGNDRTP WFCSGCPHNT STRVPEGSRA
VAGIGCHYMT TWMPDRNTST FTQMGGEGVT WVGQSPFTQE AHVFANLGDG TYFHSGLLAI
RQSIAAGVNI TYKILYNDAV AMTGGQTVGE RPEGHSVAQI AHSLRAEGVV KLVVVTDDPS
KYHGRTHHID ANPARAQHQE LINDLPAGIE VFHRDELDRI QREFRAIPGC TAIIYDQTCA
TEKRRRRKRG TLATPDKTVV INELVCEGCG DCSVQSNCLS VEPVETPFGR KRRINQNTCN
KDYSCVNGFC PSFVTVEGGT LKKPKKEKKG DLSSLPAIPE PQLPRADTAW GIVVGGVGGT
GVITIGSLLG MAAHLEGKGV ITQDAGGLAQ KGGATWSHIQ IANRPEAIYT TKVDMAKADL
VIGCDPIVAA NKASLAVMQN GRTFVALNSH GTPTAAFVHN PDWQFPGGSC EAAIAGAVGP
GLVGCFDAEQ AAVQLLGDSI YTNPLMLGYA WQKGRVPLTR AALMRAMELN GVQVANNQAA
FEWGRRCAHN LAEVEALYRT AQVIQFVKKT GLQELVAQRE QFLTGYQNAA YAAQYRSFVD
QVQAAEGRLG SSTRLTEAVA RYLFKLMAYK DEYEVARLHT DPAFTAKIAD MLEGDYKLVH
HLAPPLSAAK DAQGHLVKKS YQPWIRSAFG VLAKLKGLRG TPLDLFGRTA ERRTERALIV
EYRDCITQLL PQLTADKLEL AVQIARIPED IRGYGHVKER HLAAARSKWQ GLMQQWQAPQ
PGAQHRA
//