ID A0A2C9T3N0_9MYCO Unreviewed; 1255 AA.
AC A0A2C9T3N0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:GAY18415.1};
GN ORFNames=MSZK_51410 {ECO:0000313|EMBL:GAY18415.1};
OS Mycobacterium sp. shizuoka-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY18415.1, ECO:0000313|Proteomes:UP000223528};
RN [1] {ECO:0000313|EMBL:GAY18415.1, ECO:0000313|Proteomes:UP000223528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA Hoshino Y.;
RT "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL Submitted (OCT-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:GAY18415.1}.
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DR EMBL; BEWG01000104; GAY18415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9T3N0; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000223528; 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; 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.
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:UP000223528};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 1..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 727..865
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 889..1104
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1255 AA; 134848 MW; BD9368CE893DCDC9 CRC64;
MAISTACSYC GVGCGIDVRT TPGPDGPVIA SVVGDRLHPT NLGRLCTKGA THAELMGDTQ
GRAVSALIRP ARGAEFVEAP VADAVAAVGS RLREIADRHG PDSVALYVSG QMSIEAQYLA
TKLAKGFLRT VNLESNSRLC MASAATGYKR SLGADGPPGS YADIDCADLF FVIGANMADC
HPILYLRMAD RLRAGAKLIV VDPRRTATAA DADLFLQIRP GTDLALLNGL LHLLVAGGDI
DTDFIAEHTE GWAAMPEFLA DYPPARVAEL TGLREADIRA AATMIAAAGQ WMTLWTMGLN
QSAHGTDNTS AVCNLHLATG AICRPGSGPL SLTGQPNAMG GREMGYLGPG LPGQRSVASA
EDRAFVESVW GRRPGTIRSE TNRGTIDMFE QMAAGDIKAC WIICTNPVAS VPNRATVVAG
LQAAELVVTQ DAYADTATNR YADIVLPAAL WAEADGVMVN SERTMTLVRQ CVSPAGQARP
DWQLICGVAR EMGFGEHFDY QSSEQIFDEI RRFANPRTGY DIRGISYRRL RRAPVQWPCP
PGDTENRHPI RYLNPGPGPR LVFPTPSGRA VFHPCPHLPA RELPDDDYPF VLNTGRLPHQ
WHTMTKTGRV GLLTALTGNP FVEIHPGDAA ALAITDGQAV ELVSRRGRAV LPAVVTDRVQ
PGSCFAPFHW NDVHGENVTV NAVTTDAVDP DSLQPELKVC AVRLAPVGPV PTPRPPRRSA
PLPTGAPVVL WASQTGNAED LATGIVNHFA AQGIHAELAA MADVDPAALT DVGHLLVVTS
TFGDGGPPDN GIEFWDRLRA PDATALPGLR FAVLGIGDRS YGQFCGHAQA LDARLADLGG
ARLLERGECE IHDDGAIAGW IQRIMRLVNP AAAQISTQPA TTAQPFTRAN PVAARLSRNI
ALTPASAAKE VRQFGFDISE HDLGYAVGDS LGVLPTNSAA DVADWLSATG LSGEQIVEID
GTHCTLREAL TTRYDICRLT PNLLTFLADA APDKATARHL RAALADLDVW RLGRNGIDVI
RAFGVRAELE QWQDALIRLT PRFYSISSSP LVSPHEVQLT VSVVRYRGPG GAPRGGVCSS
YLADRAGATT TPIFLQRSPH FRPPRDRDAP VVMIGAGTGI APFRGFLQER RALGHTGRNW
LFFGDRHRAE NFYYRDDLTD MVTDGFLNRL DLAFSRDQAK RIYVQNKMIE AGAQLWRWLQ
DGAHLYVCGD AAAMAAGVDS ALSAIIATHG RLSTEAARDY KRELVATKRY LRDVY
//
