ID U5WAW9_9ACTN Unreviewed; 768 AA.
AC U5WAW9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative molybdopterin oxidoreductase {ECO:0000313|EMBL:AGZ45071.1};
GN ORFNames=AFR_34065 {ECO:0000313|EMBL:AGZ45071.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ45071.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ45071.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ45071.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; CP006272; AGZ45071.1; -; Genomic_DNA.
DR RefSeq; WP_023561408.1; NC_022657.1.
DR AlphaFoldDB; U5WAW9; -.
DR STRING; 1246995.AFR_34065; -.
DR KEGG; afs:AFR_34065; -.
DR PATRIC; fig|1246995.3.peg.6893; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_11; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746}.
FT DOMAIN 39..95
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 84241 MW; E0A29600DD7DF038 CRC64;
MADRIADPWG ERTPYGPGQT WPARVDLHLA EGVEEADVDR WVQSASILHS NGDAMDIAVK
DGRIVGVRGR AEDRVNRGRL GPKDLYGWQA NNSPDRLTRP LIRQDGRLVE TDWDTAMGRI
VHRSRELLEG PGGWGHFGFY TSGQLFLEDY YTLGLIGKAG LGNPHMDGNT RLCTATAAAA
LKASFGTDGQ PGSYTDVDHC DTIAVWGHNP AETQAVLWMR MLDRRSGPNP PALLAVDPRS
TPVAREADVH LAPRTGTNQA LLNGLLREII QRGWCDDTYL AAHTIGFDEL SRVVDACPID
RVAGICDLKA ADIERAAEVI GTAGRLLSTV LQGFYQSNQA TAASCQINNL HLVRGQLGRP
GAGVYQMNGQ PTAQNTRETG ADGDLPGLRN WDNPDHIREL AELWNVDDLT IPHWSPPTHA
LQIWRYAEQG SIKLLWISAT NPAVSLPDLA RIRRILAQPE LLVVVQDLFL TETAELADVV
LPAATWGEKT GTFTNADRTV HLSEKAVDPP GEARADLDIF LDYARRMDFR NRDGEPLIGW
TTPEEAFEAW KWCSAGRPCD YTAITYERLR GGSGIQWGGE RLYTDGVFNT DPGYCETYGQ
DLSTGAEFTA EQYRAKEPAG RAFLHAADYQ PSPEVPSGDF PLLLTTGRTI YQFHTRTKTG
RAPELDAAAP DVWVELHPDD AARYGITEGD LVNISSPRGG IEARARLGGI RLGVVFVPFH
YGYFDVDPAG RRPRAANELT VTAWDPVSKQ PIFKVAAVRI AKLAGPEG
//