ID A0A0J8AVE8_9SPHN Unreviewed; 1161 AA.
AC A0A0J8AVE8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:KMS58175.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:KMS58175.1};
GN ORFNames=V473_08455 {ECO:0000313|EMBL:KMS58175.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS58175.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS58175.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS58175.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
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:KMS58175.1}.
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DR EMBL; JACT01000001; KMS58175.1; -; Genomic_DNA.
DR RefSeq; WP_066602427.1; NZ_KQ130434.1.
DR AlphaFoldDB; A0A0J8AVE8; -.
DR STRING; 1420583.V473_08455; -.
DR PATRIC; fig|1420583.3.peg.1697; -.
DR Proteomes; UP000052232; Unassembled WGS sequence.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 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:KMS58175.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052232}.
FT DOMAIN 725..910
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 939..1134
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1161 AA; 125675 MW; 96C5A85192B6D958 CRC64;
MRDVKLDDKY TVDDGRVIMS GTHALIRVPL LQKEIDQRNG LDTGGFISGY RGSPLGSYDM
ELWRAKKLLE SHDIIFQSGV NEELAATAVW GTQMLATTPG ANKDGVFAIW YGKGPGVDRS
GDPFKHGNIA GTHPHGGVLI VAGDDHSGKS STVAHQSEVA LMHAGMPILA PSNVQDVIDL
GLLGFAMSRY TGLYTGFKLT NETLEQTMTV DIRVGGHGPV TPDRGPAPAN GFHNYPTHLD
RTASEIVVKR YRWPLVEKFV RANGIDRVLI DTPARRLGIV TTGKAVQDVR QALKLLGLDD
AAAAAMGLGV YKLGCMYPVE REGLAEFAAG QSELLFIEEK DPLTENQAKA ILYGRLAMPR
IVGKVDEDGV FMIPSDEQLE PVQLALVIAE RLRRLGVADE ALAVRAEILS RQMETVKGLK
PADAARSPYF CSGCPHNTGT RFPEGSIAAG GIGCHAMAMY SGPDMLPNAQ MGGEGAHWYS
LAYFSDMNHI FQNMGDGTYY HSGLLAVRGA VAAKVNITFK ILFNDAVAMT GGQPVDGPLT
PGDITRQVLA EGAVRCIVVT DRPDLYGAHS GLGEGVTVHH RDTYDAVQKE LRDVPGVTVI
VYEQTCAAEK RRRRKRGKFP DPAKRMFVNA AVCEGCGDCS VQSNCVSVWP KETELGRKRQ
IDQSNCNKDY SCVKGFCPSF VTVLDAEPRK PKKAQLDGEA DMALPDPAIV PLHHGAYNIM
ISGIGGTGVV TIGALLAMAA HLEGKSTSVF DMTGLSQKNG AVFSHLRIAA HNDDLGAQKL
GIAEADLALA FDAVAGLAKE PAMTLSTERT KVVVNARVTP TPAFQRNPDL TLDQGLLVRR
LKTMSADLHG VDATGLGLAL LGDTIAANLF MLGYACQLGL LPVSPDSIER AVEINGVAIP
FNKAAFALGR FQAVDPARIE KAVVSHVQEL DFTPLTALVD IVAHRTQLLT DYQNVAWAQR
YRDLVDSVAR AEVRATPGRD MLSVMVARNF AKLMAYKDEY EVARLHADPA FRQQLKDAFE
DGAKLRYNLA PPLFSKKDAD GRLIKREFGP WMGKAFAFLT RFKGLRGTAF DIFGYTQERK
MERGLIDHYE AQMRMVADKL TPANHAAAVE LASLPAQIRG YGHVKEANVE KVRALEPLIL
KKFEDAAISA LGAPAPLVQN A
//