ID A0A132PBZ0_9MYCO Unreviewed; 1345 AA.
AC A0A132PBZ0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:KWX19838.1};
GN ORFNames=AFM11_33845 {ECO:0000313|EMBL:KWX19838.1};
OS Mycolicibacterium wolinskyi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX19838.1, ECO:0000313|Proteomes:UP000070612};
RN [1] {ECO:0000313|EMBL:KWX19838.1, ECO:0000313|Proteomes:UP000070612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC_01 {ECO:0000313|EMBL:KWX19838.1,
RC ECO:0000313|Proteomes:UP000070612};
RA de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA Limbago B.M., Noble-Wang J.;
RT "A draft genome sequence of Mycobacterium wolinskyi.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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}.
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:KWX19838.1}.
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DR EMBL; LGTW01000035; KWX19838.1; -; Genomic_DNA.
DR RefSeq; WP_067858903.1; NZ_LGTW01000035.1.
DR STRING; 59750.AWC31_07540; -.
DR PATRIC; fig|59750.3.peg.5107; -.
DR Proteomes; UP000070612; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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 CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR CDD; cd06199; SiR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.360; -; 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 Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070612};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 8..68
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 817..951
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 982..1213
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1345 AA; 146157 MW; DE9E49400EF45628 CRC64;
MADGATLAAT RRTACSYCGV GCGIEVSTRV EDGRTVIARV AGDKLHPANF GRLCTKGATH
ADMMAADDDR LKSALLRPTR DDELTPTPVD DAVAEAARRL RAIIDEHGPD AVALYVSGQM
SIEAQYLATK LAKGFLRTVH IESNSRLCMA SAGTGFKQSL GADGPPGSYG DFDCTDLFFV
IGSNMADCHP ILFLRMADRL KAGAKLIVVD PRRTATAEKA DLFLQIKPGT DLALLNGLLH
ILVENGDIDA EFIAEHTTGW DTMPQFLADY PPARVAEITG IPEDDIRTAA AMIAEAGEWM
TCWTMGLNQS THGTWNTNAI CNLHLATGAI CRPGSGPMSL TGQPNAMGGR EMGYMGPGLP
GQRVVLSADD RAFVEAQWGL EPGTIRSEVG PGTVGMFEQM AAGDIKACWI ICTNPVASVA
NRKTVINGLE AAELVVVQDA YRATATNHYA DIVLPAALWA ESEGVMVNSE RNLTLLSPSL
PPVGQARPDW KLICEIAAHL GFAEHFDYTC AEEIFDEIRR FANPKTGYDL RGASYERLRR
TPLQWPCPPA DAPGGDTDRH PIRYLNDGVS QDLFVDETGH RPRLAFPTPS RRAVFHARPH
MDAAELPDDD YPMVLNTGRL QHQWHTMTKT GKVAGLNKLN PAPFIEIHPI DALELEIVAG
QPVEVASRRG RAVLPAVLSD RVRPGNCFAP FHWNDEHGEY LTVNAVTNDA VDADSLQPEF
KVCAVSLRPA RSVGGAGYTH PVAAELGVTT DLKPGLTEAE KTYLAGFFTG LPDSPAGVPV
LPGSAPVSPK VRLWVDGVLA GRYSRTSVAE RSVPTGPLVL WASQTGNAEE FAAKLATRLD
GATLVNMDDL ALGELAAARD VLVVTSTFGD GGPPDNGADF WSRLEAPDAP ELHGMRYAVL
GIGDRAYDNF CGHAKSLDRR LADLGATKLL DRTECEAYDD GPMQQWADTV TELLTGQPTE
PPGRPVGGRT VIRTEPDEFT RAKPILATLS RNTVLTAPGS AKEVRQFGFD ISDYDVNYSA
GDSLGVYATN DPAVVDAWLA ATALNGDAVV EVDGTEQSLR DALISSYDIC RVTPNLLRFV
ADSCTDRSAK VLRGSGERLK KWLRNRNALD VVTEFGVHAE PEQWQEVLVR LTPRNYSISS
SPLVSPHEVQ LTVSVVRYPG AQGGVRGGVC STFLADRAAA APVFLQRSPH FRPPEDAATP
MIMVGPGTGI APFRAFLQER RALGHTGRNW LFFGDQHRNE NFYYRDDLED MVHDGFLNRL
DLAFSRDQAK RVYVQHKMLD YGADVWRWLD DGAHFYVCGD AGRMAKDVDA ALTTIIRTHG
GISEERARDY KRELVAEKRY VRDVY
//