GenomeNet

Database: UniProt
Entry: A0A132PBZ0_9MYCO
LinkDB: A0A132PBZ0_9MYCO
Original site: A0A132PBZ0_9MYCO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system