ID A0A1X0K011_9MYCO Unreviewed; 1253 AA.
AC A0A1X0K011;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ORB68503.1};
GN ORFNames=BST47_00860 {ECO:0000313|EMBL:ORB68503.1};
OS Mycolicibacterium tusciae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=75922 {ECO:0000313|EMBL:ORB68503.1, ECO:0000313|Proteomes:UP000192411};
RN [1] {ECO:0000313|EMBL:ORB68503.1, ECO:0000313|Proteomes:UP000192411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44153 {ECO:0000313|Proteomes:UP000192411};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) 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:ORB68503.1}.
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DR EMBL; MVIM01000001; ORB68503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0K011; -.
DR STRING; 75922.BST47_00860; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000192411; 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 Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 1..61
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 738..871
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 892..1121
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1253 AA; 137175 MW; 152EF17C331E67C5 CRC64;
MTVTRTACSY CGVGCGITVE TTTDDGRAVI ARVSGDKLHP TNFGRLCTKG STHAEMMAAV
DGRLTSALLR PARGEEAVPV PVDDAVAEAG RRLRAVVDEH GPDAVALYVS GQMSIEAQYL
ATKLAKGFLR TVHIESNSRL CMASAGTGYK QSLGADGPPG SYTDFDCADL FFVTGSNMAD
CHPILYLRMV DRLKSGAKLI VVDPRRTATA ERADLFLQIR PGTDLALLNG LLHLLVENDD
IDADFIADHT EGWETMPAFL ADYTPEVVAQ ITGLAEEDIR TAAKMIGEAG EWMSCWTMGL
NQSTHGTWNT NAICNLHLAT GAICRPGSGP MSLTGQPNAM GGREMGYMGP GLPGQRSVLS
AADRAFVERQ WGLEPGSIRT DVGPGTIDMF SQLADGRIKA CWIICTNPVA TMANRATVIA
GLEVAELVIT QDTYRETATN RYADIVLPAS LWAESDAVMV NSERNVTLLA QSLPPRGEAR
PDWQLICQVA THLGFGEYFA YESSEQIFDE IRRFSNPKTG YDLRGVSYAR LRETSLQWPC
PPGDDNDRHP IRYLNDGISQ DYFVDENGHA PRLAFPTPSR RAVFHARPHM NPRELPDDDF
PMVLNTGRLQ HQWHTMTKTG KVDALNRLNS GPFVEIHPLD AVALDIVGDQ PVELSTRRGR
AVLPSVVTDR VRQGTCFVPF HWNDEHGEYL TVNALTNDAV DPDSLQPEFK ACAVSLRPFA
APLRKTKPLT PPELTEGPLV LWASQTGTAE EFAGKVAAAI GVTNLVNMND MALADLATRD
VLIVTSTFGD GGPPDNGAEF WSRLNSPDAP TLTGVRYAVL GIGDRTYDNF CGHAKAIDTR
LVALGAARLL ERVECEAYDD EPMSRWVDQV AGLLGRSVSS THAAVAAPFT RAHPIVAPLC
RNVLLSSASA LKEVRQFGFD ISGFDVGYAA GDSLGVYPTN DPAAVDAWLA ATGMHGEHTV
VVDGTEQSMR EALTSRYDFC RVTPDLLRFI TENSRDAKAL RASKDKLDKW LVGRNGVDLV
QEFVVHADPD QWLEVLVRLT PRNYSISSSP LVSPHEVQLT VSVVRYRGAD GGRRGGVCST
FLADRATTAP VFLQRSPHFR PPEDSGTPMI MVGPGTGIAP FRGFLQERRA LGHAGRNWLF
FGDQHRSENF YYRDDLEDMA RDGFLSRLDV AFSRDQAKRV YVQHKMLDRG ADVWRWLDDG
GHFYVCGDAS RMASDVDAAL TAIIEKHGGM SRERAHDYKR ELVAAKRYVR DVY
//
