ID A0A136N5L6_9BACT Unreviewed; 622 AA.
AC A0A136N5L6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein {ECO:0000313|EMBL:KXK41455.1};
GN ORFNames=UZ11_BCD004001997 {ECO:0000313|EMBL:KXK41455.1};
OS Bacteroidetes bacterium OLB11.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617422 {ECO:0000313|EMBL:KXK41455.1, ECO:0000313|Proteomes:UP000070496};
RN [1] {ECO:0000313|EMBL:KXK41455.1, ECO:0000313|Proteomes:UP000070496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB11 {ECO:0000313|EMBL:KXK41455.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK41455.1}.
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DR EMBL; LNFQ01000066; KXK41455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136N5L6; -.
DR STRING; 1617422.UZ11_BCD004001997; -.
DR PATRIC; fig|1617422.3.peg.2171; -.
DR Proteomes; UP000070496; 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; 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; 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};
KW Pyruvate {ECO:0000313|EMBL:KXK41455.1}.
FT DOMAIN 20..211
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 261..474
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 622 AA; 68527 MW; 505F57C5A798090A CRC64;
MSNLIQELEQ VVIKFAGDSG DGIQLTGSQF TNNTALVGND LSTFPDFPAE IRAPIGTVPG
VSGFQLHFSS KPIYTPGDKC DVLVVMNAAA LKVNLKVIKK GGIIIANTDG FDTKNLRLAK
YEEGENPLEN ESLSSFQVYK IDVTKLTREA LKDITTLGVK EKDRAKNMFV LGLLYWIYDR
DMSNTEKFLN KKFGKQADVL QSNLLALKAG YYYGETAEIF TSQYKVAKAQ VEPGTYRGIT
GNVALALGLV AASQKMKLPL FLGTYPITPA SDILHELSKY KNFGIMTFQA EDEIAGITTA
IGASYGGSLG VTTTSGPGMA LKTEAMGLAI MLEIPLVIID IQRGGPSTGL PTKTEQSDLL
QAYYGRNGES PMPVLACATP SDCFQMAIEA CRIAVQHMTP VILLSDGYIA NGAEPWRFPT
SKDLPDIDVK FKKHLDEGEE KLMPYKRNEQ LVRPWVLPGY AHLEHRIGGL EKQDITGNIS
YDPDNHQHMV KTRQQKIDLI SDNIPLQTIT NGADKGKVLL LGWGSTYGVL SVVSQNLIAQ
GFSVSHCHLK YIRPFPKNIS EILNNFETVI IPEINNGQLI RIIKSEFMIH AIPFNKIKGT
PITQAELEEF VLTYLTNQNE YE
//
