ID F1Z348_9SPHN Unreviewed; 1361 AA.
AC F1Z348;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:EGD60965.1};
GN ORFNames=Y88_3469 {ECO:0000313|EMBL:EGD60965.1};
OS Novosphingobium nitrogenifigens DSM 19370.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD60965.1, ECO:0000313|Proteomes:UP000004728};
RN [1] {ECO:0000313|EMBL:EGD60965.1, ECO:0000313|Proteomes:UP000004728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD60965.1,
RC ECO:0000313|Proteomes:UP000004728};
RX PubMed=22156397; DOI=10.1128/JB.06381-11;
RA Strabala T.J., Macdonald L., Liu V., Smit A.M.;
RT "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T.";
RL J. Bacteriol. 194:201-201(2012).
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:EGD60965.1}.
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DR EMBL; AEWJ01000002; EGD60965.1; -; Genomic_DNA.
DR RefSeq; WP_008071908.1; NZ_GL876935.1.
DR STRING; 983920.Y88_3469; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_000422_6_2_5; -.
DR InParanoid; F1Z348; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000004728; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
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; PS00932; MOLYBDOPTERIN_PROK_3; 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:UP000004728};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 3..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 831..967
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 994..1210
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1361 AA; 146913 MW; 07E1BE36C1F2CE8C CRC64;
MTTKQAKSVC PYCGVGCGIV FDVAEGRIVK VSGDKSHPAN FGRLCTKGNS CHVPVTAEGR
ADRAYVRLSE GRDHGAVPMD EAIARTAQGL RTIIDRDGPD AVSFYVSGQM SIEAQYLANK
LCKGFIGTNN IESNSRLCMA SAATGYKLSL GADAPPGSYQ DFDKADLFFV IGANMADCHP
ILFLRMMDRV KAGAKLIVVD PRRNATADKA DLFLQVRPGT DLALLNGLLR LLVENDAIDR
DFIDLHTQGW DAMPAFLADY DVDTVAGITG LAPDDLRKAA QWIGAAGAWM SCWTMGLNQS
THGTWNTNAI CNLHLATGAI LKPGSGPFSL TGQPNAMGGR EMGYMGPGLP GQRSTMSEAD
RAFVEAEWGI APGTLRKEAG QGTIAMFDDM AAGQIKACWI ICTNPVASVS NRAKVIAGLE
AAELVITQDA FLETETNRFA DIILPGALWA EADGVMINSE RNMTLARQAV APPGEAMADW
EIIARVACAM GYAKAFTYAN AAEVFDEIRR FSNPATGYDV RGVSHQRLRE TPLQWPCPPE
GESDRNPIRY LNDGISQTLR RDEDGTVPPV AFPTPQGRGI FLARPHMAPA EMPDGDFPMV
LNTGRLQHQW HTLTKTGKVP TLNKLNPGPF VELHPDDAQE LGIADRDRVE VRSRRGRAVL
PAVVTDRVAP GACFAPFHWN DVFGEDLCIN AVTSDAIDAQ SMQPEFKFAA VALTRVGGPI
EDETAGTAPA PLAHLPESAS MPDIADVLAG FLRLPSRPPE FPEQEQQYLA GFVAGLRLDT
APCADAMPIV PDNAPLARER RDYVNGLLAG MLARVPVARA MPGTVAHGPE IRVIWASQTG
TTESYAEHCA AELTRRGFAV RLCPMDDVTP GDLAGPALFL ASTFGDGDPP DNGATFWQAL
SSPTAPECPD LAFAVLAFGD SSYDRFCGFG QALDARLAEL GGTRLIARVD CEPDYEDAAA
AWLDAVAGTL APAGAEPVVA EAKAAPAGAK YGRKTPFSTA LVTNRLLSGA GSQKEVRQFG
FDLADSDFSY EAGDALGVWP SNCPDLAAEL IARVGASPDA AVVVPGQGEM PLDEALVRHL
DIARVSRSFL EMVAEHRPDA PFAPLLAQDR KADCENWTYG RQVPDVLDHA PLVLSGQDLV
DALKPLQPRL YSISSSPRVC PDEVQLTVSV VRWMQEGRLR KGVCSSYLAD RAGGEASRIF
LQASPHFRPP ADTDRPAIMV GPGTGIAPFR AFLQDRQAQG AGGANWLFFG EQHAASDFYY
HDEIEAWHRD GHLDRLSLAF SRDTAQKVYV QHRMIEEGAQ LWRWLAEGAH FYVCGDASRM
ARDVDTALHR IIADHGNMTE DAARDFVTAM QKDKRYVRDV Y
//
