ID L7LJ94_9ACTN Unreviewed; 1355 AA.
AC L7LJ94;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Putative nitrate/sulfite reductase {ECO:0000313|EMBL:GAC61200.1};
GN ORFNames=GSI01S_15_00700 {ECO:0000313|EMBL:GAC61200.1};
OS Gordonia sihwensis NBRC 108236.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC61200.1, ECO:0000313|Proteomes:UP000035083};
RN [1] {ECO:0000313|EMBL:GAC61200.1, ECO:0000313|Proteomes:UP000035083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC61200.1,
RC ECO:0000313|Proteomes:UP000035083};
RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL Submitted (DEC-2012) 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:GAC61200.1}.
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DR EMBL; BANU01000015; GAC61200.1; -; Genomic_DNA.
DR RefSeq; WP_006896602.1; NZ_BANU01000015.1.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0369; Bacteria.
DR Proteomes; UP000035083; 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:UP000035083};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 8..64
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 823..959
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 992..1204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 711..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1355 AA; 144767 MW; 5AB723BE449102ED CRC64;
MSLEPLAPTA VDTVCGYCGV GCGLTLDVAD GAVTGARGTK SHPANRGRLC TKGATTADML
RAPGRLTTAL IRERRDGDAR PADVDDAIAE TARRLTRIRD RHGPESIAVY VSGQMSLEAQ
YLANKLVKGF LGTNQIESNS RLCMASAGTG YKQSLGADGP PGSYDDIDHA DAFLVIGSNM
ADCHPILFLR LLDRVAAGAR LIVVDPRRTA TASKAHIHLP VRPGTDLALL NGLLRLIVDE
GGLDEEFVAA HTRGWDALAA MLDDYPPERV AELTGVDEDA LRETARILAG AENWMTLWTM
GLNQSTHGTW NTNAVCNLHL ATGTICRTGS GPFSLTGQPN AMGGREMGYM GPGLPGQRSA
LDAGDRADVE AAWGLEPGTL STDPGGGTVD MFEAMADGRI RAAWIICTNP VASVANRSTV
VQALRRADFV VVQEAFTGTE TCEYADIVLP AALWTEAQGT MVNSERSISL TSPAVAPPGQ
ARADWELISQ IARGMGFRDG FSHADAAAVF DEIRGFHNPR TGWDLRGVDY ARLREGPVQW
PAAPGGPARN PIRYLSDDPA EPGPLFPTPD RRARFLARPH MPPAELPDDD YPMVLTTGRL
AHQWHTMTKT GRVAKLCRLD PGSFVQIHPD DARPAGIGDG DMVEVRSRRG AVRVPARVDD
AVSAGVCFVP MHWSDAFGEM LAVNAVTTDA VDPDSLQPEF KACAVALTRL SGPVPDNQEP
PMTTADPTAA DPTATESSSL AVALRVDAGE PVLTETERGY LAGLLRGLTA NPPRDAVPTV
PSQAPLSEPA RIWVDGVLAG YFSRVPMTGP GSASVVDSPA RRIRLVWASQ TGTAEEYAAQ
CAGALRDAGF DVIDASAERT GLGDLVGDVL FIVSTTGDGD APDAAVGLWD ALAGACAQDV
DGLRFSVLGF GDSSYADFCG FARKLDARLA TLDAQRIAPA GYCEPDYDTA AAAWLAGVVA
VLDSPASPDD PDTAADSRTC AESPPAPGYS RKNPFTARVL ENAVLTTGTA KEVRRIAFHL
PPGSLEYTAG DALGVWPRNS ETLVDEWLAR TGLDGAEAVT VDGAPVPLRQ ALTEDYEIAD
CSRDLVAFVA ERTGDSELRA LLDDPAGFAD WAWNRQSVDL LATHPVSATA AQWLSVCRRL
RPRLYSISSS PSAHPERVEA TVSVVRFGDE SAPRRGVCSG FLADRGPADL ARIFITPNKK
FGPPVDPEAP AIMIGPGTGI APFRAFLHER AASGAAGDNW IFFGERHRAT EFYYEDELAG
FREAGVLTRL DTAFSRDQPE KVYVQHLMRE RAPEIWEWLR RGAHVYVCGD AKHMARDVDD
TLKQIVAEHG RLAPSGAENY LRALSAEGRY VRDVY
//
