ID A0A0E4HG89_9BACL Unreviewed; 1410 AA.
AC A0A0E4HG89;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:CQR58952.1};
GN ORFNames=PRIO_6605 {ECO:0000313|EMBL:CQR58952.1};
OS Paenibacillus riograndensis SBR5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC Paenibacillus sonchi group.
OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR58952.1, ECO:0000313|Proteomes:UP000033163};
RN [1] {ECO:0000313|Proteomes:UP000033163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (MAR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN831776; CQR58952.1; -; Genomic_DNA.
DR RefSeq; WP_020434412.1; NZ_LN831776.1.
DR STRING; 483937.AMQ84_31065; -.
DR KEGG; pri:PRIO_6605; -.
DR PATRIC; fig|1073571.4.peg.7063; -.
DR HOGENOM; CLU_000422_6_1_9; -.
DR Proteomes; UP000033163; Chromosome I.
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:0016651; F:oxidoreductase activity, acting on NAD(P)H; 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; 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.
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 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 860..998
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1042..1259
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 828..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 154099 MW; F150562E913FA755 CRC64;
MTTGKVKSVC PYCGVGCGII LEVSGNRVVS ITGDKEHPAN FGRLCTKGST AAAALTESGR
MEYAYKRQDR GAGPERVKID EAIRDTAQRL RAILEEHGPD ALSVYVSGQM SLEAQYLINK
LAKGFIRTPN IESNSRLCMA GAGNGYKLSL GADGPPGSYQ DMDKTDLFFV IGANMADCHP
ILFLRMMDRV KAGAKLIVVD PRRTATADKA DLFMQIRPGT DLALLNGLLH LLVKNGHTDP
AFIARFTSGF ESMEAFLEDY PPDKVSEITG IPEADIRQAA EWIGGAPEWM SCWTMGLNQS
IHGTWHTNAI CNLHLATGAI CRPGSGPFSL TGQPNAMGGR EMGYMGPGLP GQRSLVSEAD
RSFIEKLWEI PQGTLRSDAS GGTISMFESM IAGRIKACWI ICTNPVATVP NRKKVIAALE
AAELVITQDS FLDTETNRYA DILLPGALWA EGEGVMINSE RNLTLMQQAV EPPGEAMPDW
QLIARVAAEM GYAGAFAYQS SAEVYAEIQQ AWNPKTGYDL RGATYARLRE TPVQWPSAPD
QPNDRNPIRY LNRQGGTALN EPADGSVPDI VFPTDSGKAV FWARPYMPPA EMPDSDYPFV
LNSGRLQHQW HTLTKTGKVP KLNKLNPGPF VEIHPEDAEA LGIKDRQPVE LRSRRGQAVL
PAVLSDRVRP GNCFAPFHWN DVFGAQLAVN DVTNDAVDPL SLQPELKFCS VSLVKAAGQL
SGEPQAPDMG GNQPVPPAAA ENAHLKEAVT MKQLDALAGL FGLEAPTAMT LDRREQAYLS
GFITSLRTEA GRSASGIPVL PATAPFEPST RYFVDGLLAG MFSRTPLPGA EPHSRQVMPS
GPASSGAASE EAEAAGKLPV TILWASQTGN AEGAAIDCAK KLQQAGYDIR LVNMNQYSVS
DLAKTRFALF IASTFGAGDP PDNGESFYQA LRAENASLLK DLRYAVLAFG DSNYDLFCGF
GKNLDTRLEE LGASRLLDCA HCDTDYQEQA DAWTKDISEL LRGFTGRPEP SGLAAASGIS
SASIAASGPA SPNPDQRGYH RNHPVPSRLL FKQQLNKAGS EKETRHYAFD LKSAGVQFEA
GDALGVWPVN CPGLVDDLLH TLDIEPSAPV MVAGQGELPV NEALHRHFEI ARIAPEMLRF
IRDRTQNRQL IKLLQSENQT ELKQWLWGRQ LIDVLQEFPV ALSAQEFLEQ LKPLQPRLYS
ISSSPKAHPD EVHITVSTVR YGNNGNVRKG VCSTFLADLA TEDTEIPIFI QKNAHFRPPV
NPDAPMIMVG PGTGIAPFRG FLQERKASGA KGKNWLIFGE QREDSDFYFR GELEAFREEG
FLQRLDTAFS RDQAEKIYVQ HRILEHGAKI WAWLQEGAHF YVCGDARQMA KEVDAALKTV
IRQHGGRTAD EAHDYVKEMS LTKRYVRDVY
//
