ID A0A0V8S4P9_9CELL Unreviewed; 1421 AA.
AC A0A0V8S4P9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Reductase {ECO:0000313|EMBL:KSW15277.1};
GN ORFNames=ATM99_01880 {ECO:0000313|EMBL:KSW15277.1};
OS Cellulomonas sp. B6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW15277.1, ECO:0000313|Proteomes:UP000054319};
RN [1] {ECO:0000313|EMBL:KSW15277.1, ECO:0000313|Proteomes:UP000054319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:KSW15277.1,
RC ECO:0000313|Proteomes:UP000054319};
RA Piccinni F.E., Campos E.;
RT "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT Isolated from Decaying Forest Soil.";
RL Submitted (NOV-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:KSW15277.1}.
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DR EMBL; LNTD01000229; KSW15277.1; -; Genomic_DNA.
DR RefSeq; WP_062103953.1; NZ_LNTD01000229.1.
DR STRING; 1295626.ATM99_01880; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000054319; 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 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:UP000054319};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 14..71
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 852..989
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1049..1270
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 992..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 150674 MW; 74D8C19337F49F3C CRC64;
MTATTTARDE RTATTQVATV CSYCGVGCGI VLDVGDDGTV RRASGDRSHP ANAGRLCTKG
ATSATMLAAG GRVTTALVRP ERGTEPVPAD VDVAVADVAR RLRAILDRDG PDAIALYVSG
QLSIEAQYLA NKLAKGYLRT RWIESNSRLC MASAGTGYKL SLGADGPPGS YDDLDHADVF
LLVGANMADC HPVLFLRLLD RVKAGARLIV VDPRRTATAE KADLFLQVRP GSDLALLNGL
LHLLVEAGAV DEEFVAEHTE GWDAMPAFLA DYPPDVVERL TGVPAADLRA AAAMIAGAGD
WVSCWTMGLN QSTHGTWNTN ALVNLHLATG AIGRRGSGPF SLTGQPNAMG GREMGYMGPG
LPGQRSVLDA DDRAFCEELW DLPPGTIRTE VGTGTVDMFR RMADGEIRAA WVICTNPVAS
VGNRRTVIEG LERAELVVTQ DVFADTETNA YADVVLPAAL WSEADGVMVS SERTMTLARR
ALAAPGQALP DWQLVARVAT AMGFDGFAYA SSQEVFDELR RASNPRTGYD LRGVSYERLR
REPVQWPCAS ADAPARNPVR YLNDGAHQPL LTRPDGTRPR LAFPTPSGRA VFHARPHVDP
AELPDDDHPF WFTTGRVQHQ WHTMTKTGKV PALNRLEPGP FVEVHPEDAA RLGLVERAPV
EVASRRGRAV LPVVVTDRVR PGTLFAPFHW NDVFGEYLAV NAVTHDAVDP LSLQPELKAC
AVALTPVVGV ADGTRASDAV AGAAVDDAPA GRAGEPGPGA RALDGPATMR ALAAALGVDD
VAPPALGDDE RRYLAGFLAG LGRGADAAGG TPVLPTSAPL RGDHALWVDG VLAGMFSRTA
PPAVPPAPAR TVTVLWASQT GTAEEVAGVV AQRLADAGHT PRVVAMDDAL ADLPRRGDVV
LVTSTFGDGD APDNGTALWE ALADPQAPSF GGARFAVLAL GDPTYDRFCG HGRRLDHRLA
ELGAQRLVER LEREPGDDTA VTTWLDGLLA ALTGGTDDAP GPRDVDGPPG RAPARTAPAA
LPTAPPTAPP AASPTASSDA APPAHATRRH PGAARLVGRR RLGAPGSAKE VREILLDTAG
SPLPVPYAAG DALAVRPLTA APLVEEWCAA TGLDPGATVE HDGATLALGD ALRTRLDLGR
PTPALLRFVA ERTTRTAGDE LRRLLRTGDR AALDAWTWDR GVVDVVAAHP LDATPQEWVD
ALRTLQPRAY SISSSPLVDP ERVRLTVSVV RWAGPDGRAR GGTCSTYLAD APADAEVAVH
VQPSAHFHPP QDPDAPVVMI GPGTGVAPFV GFLAERAARG DRGESWLVFG EQHAATDFWY
RDELAAWQDA GVLTRLDAAF SRDQRQKVYV QDRLREHGPA LWSWLERGAH VYVCGDARRM
APDVDAALRD VVAREGRLDA DAAAAYLRRL AAARRYVRDV Y
//
