ID A0A0S8H5X3_9BACE Unreviewed; 617 AA.
AC A0A0S8H5X3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:KPK80583.1};
GN ORFNames=AMS27_16720 {ECO:0000313|EMBL:KPK80583.1};
OS Bacteroides sp. SM23_62_1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703353 {ECO:0000313|EMBL:KPK80583.1, ECO:0000313|Proteomes:UP000051265};
RN [1] {ECO:0000313|EMBL:KPK80583.1, ECO:0000313|Proteomes:UP000051265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62_1 {ECO:0000313|EMBL:KPK80583.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK80583.1}.
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DR EMBL; LJUQ01000238; KPK80583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8H5X3; -.
DR PATRIC; fig|1703353.3.peg.2296; -.
DR Proteomes; UP000051265; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR033412; PFOR_II.
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; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 22..210
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 257..471
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 513..588
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 617 AA; 67862 MW; AE66B3D9B72F2F10 CRC64;
MPNKPKVVEL EDVVVKFAGD SGDGMQLTGS QFSDTSAFVG NDLSTFPDYP AEIRAPSGTI
AGVSGFQVHI GHKEVQTPGD QADVLVAMNP AALKANMKWL KEGATVIIDI DNFDSKSYKK
AGYVEDPLED GSLEGHNVIK APITSLTRSA VHEFGLDNRT ADKTKNQFVS GLLYWLFNRD
IVIGEDFLKN KFRGKHDIIN ANIKVLREGY HYAETIEAIA TTFLVNPARK KKGMFRNITG
NVATAWGMIA AAEKAGKRLF LGSYPITPAS EILQEISGRK HLGVISFQAE DEIAGICSAI
GASFTGLLGV TTTSGPGLSL KSEAIGLAVM TELPIVIVDV QRGGPSTGLP TKMEQGDLLQ
ALYGRNGESP VVVLAASTPA NCFDYAYLAC KIAIEHMTPV ILLTDGYLAN GSELWHIPSM
KDMPGIEVPS LKDNNPDFYP YLRRPDKLAR YWVIPGQKGL RHRVGGLEKS DVTGEVSHDP
INHQLMVEKR DAKVKKVADF IPLQKIFGDP EGDLLVIGWG GTYGELVTAV DEIREEGKKV
SLLHFNYINP LPKNSRELLK NFKKRIVCEL NLGQFASYLR SQFPEYDYLQ YNKIQGLPFM
IRELKNKFNE LLNEIQS
//
