ID A0A117LPQ8_9BACT Unreviewed; 1074 AA.
AC A0A117LPQ8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:KUK60669.1};
GN ORFNames=XD81_0032 {ECO:0000313|EMBL:KUK60669.1};
OS Bacteroidetes bacterium 38_7.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1635292 {ECO:0000313|EMBL:KUK60669.1, ECO:0000313|Proteomes:UP000053999};
RN [1] {ECO:0000313|Proteomes:UP000053999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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:KUK60669.1}.
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DR EMBL; LGGC01000002; KUK60669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LPQ8; -.
DR PATRIC; fig|1635292.3.peg.1098; -.
DR Proteomes; UP000053999; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 486..516
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1074 AA; 120032 MW; 3935D26677621857 CRC64;
MYKITTHPIL EIPKSEKVTF QFDGHIIEAE KGFTIAAALH QAGFPVHSHS LRNRKRSLEC
GIGKCGACEM LVDGQVKRIC ITLVDEVKEV KEIPHDYRPD IIEYAKNEPI DVYKTQVVIV
GAGPAGLAAR EILREYGIDN LVVDNNSKIG GQFLMQTHQF FFFEKEKKYG GMRGFDIAQT
LAGANHEGIF LNSTVWDILE GGRIAVKEIS TDRIYYIDTE YLVVATGAVP FMPTFENDDL
PGVYTAAVVQ KMMNMQFTLL GKNVLTVGAG NIGYLTSYQL MQAGARVKAI LEAQPFEGGF
PVQANRVRRL GIPILTSHIL LKAIPNSDST GIIGAVIARC ENFHPIPGTE TVVEGIDAIN
ICTGLVSDDQ LLIKGNEIFG RKCYGAGDAI RIGEGTSAVL RGKQVAYEIL MDMGIRLNYD
EYLSLSKEYI DSQQHPIKII DQPYRPERER MEAKGFVLID CLYGFACNPC AFSCPHGAIT
KSSTSTVPSI DFNKCIGCMD CVYQCPGLAI FGYNLKRDWV FLPIEYEVKE NVEVFLVDNN
GKVLGEGVID KILRKPNKTH IARVKSFSLH GEDLTQVRSF IVKENYPEPF ELQPYDEQVP
AESYICHCDD VKMEEILEVV GERKFISIDE IKHTTRLGMG ACRGKRCIPR LKSKIKDYGI
QIVGEATPRG PMSNQLVLGE LYPRPVQENY IVNKPIKKIK VEAIIAGGGI GGSALFRYLS
EAGKKPFLIN FGRGSSWRNI AGGRPNFSVP ELSDIAEHNR QIFIELQQLR NIDYHPIQYV
NFAHDEDMYK ALEAAMAWSK AEMISPKDFT KRISPFFNPS LKTYIAAQIT YNCWQATPGK
TIDLIRQIGI QHGGTILEDC KLIDVKKNGN EFLVLVQDHT KQYIEYSTEI FINALGPEAG
QFARRLGIEA GLYPVRHQAF ITRRMPMLGV NNIPLPMLID RRKYKGFVAV YGQQLAETGQ
VIGCASPAVD PAETSKNLKI NTKEFLEIVS EVFVDWLPEL SSVGFQAIWA GYYVEPRMII
DPDLGLFVGL RGQGFMLGQY LAKMYVDKLI GRSVPEYFPR LSIQGDGLPE KAFK
//
