ID A0A0Q4R5V9_9BACL Unreviewed; 1401 AA.
AC A0A0Q4R5V9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Reductase {ECO:0000313|EMBL:KQO12451.1};
GN ORFNames=ASF12_31035 {ECO:0000313|EMBL:KQO12451.1};
OS Paenibacillus sp. Leaf72.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO12451.1, ECO:0000313|Proteomes:UP000051722};
RN [1] {ECO:0000313|EMBL:KQO12451.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO12451.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO12451.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO12451.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KQO12451.1}.
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DR EMBL; LMLV01000009; KQO12451.1; -; Genomic_DNA.
DR RefSeq; WP_056035673.1; NZ_LMLV01000009.1.
DR STRING; 1736234.ASF12_31035; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000051722; 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: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; 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:UP000051722};
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 863..1001
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1033..1250
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1401 AA; 154296 MW; A01BE70DBEEFFF3C CRC64;
MPTEKIKSVC PYCGVGCGII LEVSENRVIK VTGDKEHPTN FGRLCTKGNT CAEAISESGR
MEYAYERLSR KGELQKLAID EAISKTAAQL RSILDEHGPN ALSFYVSGQM SLESQYLINK
LAKGFVGTNN IESNSRLCMA SAGSGYKLSL GADGPPGSYQ DFDQSDLFFV IGANMADCHP
ILFLRMMDRI KAGARLIVVD PRRNATADKA SLYMQIKPGT DLALLNGLLH LLVKNNDIDE
AFIADFTSGW EPMIAFLDDY PPDKVAEITG IPEEHIRKAA AWIGESPNWM SCWTMGLNQS
THGTWHTNAI CNLHLATGKI CRPGSGPFSL TGQPNAMGGR EMGYMGPGLP GQRSVLVEKE
RDFIESLWRL PSGTLTTEVG TGTVSMFEQM QAGQIKACWI ICTNPVVTVP NRRNVIAGLE
KAELVITQDA FLETETNAYA DIMLPGALWS EAEGVMINSE RNLTLMQKAV KPPGEVLPDW
QIIARVACEM GFADAFSYSS SEEVYQEIQQ AWNPKTGYDI RGASYERLRS TPLQWPCAPE
SEADRNPIRY INNGISQTLK LKEDGSLPRL VFPTESGKGI FLARPFLPPA ELPDMEFPFI
LNTGRVQHQW HTMTKTGKIA KLNKLNPGPF VEIHPEDAAT LGITADNQVE IRSKRGVAIL
PAVITDRVRP GNCFAPFHWN DIFGKNLAIN DVTNDAIDPI SFQPEFKFCA VSLIRVAASA
EAAPIIHSDE EITASHSAFR SASNVYEEEI YMSKVDTLAS MLGIESTSVM TLENHEKTYV
TGFIASLKTS ELQSAPGIPV LPPSAPLEAS KKLFLDGLLA GMFSRTYLSE SGAALSAAAS
TGQATLEPPV PFVHIKDAEA LRITIVWASQ TGNAEEAAQA CAKQLLAAGH HVQLLNMDDY
DIKNLANEQY VLCIASTFGA GDPPDNGTGF WHSLQADDAP KLPGVTFAVL GFGDSSYDLF
CGFGQQLDAR FEHLGAKRLM PRTDCDTNFQ EQVSAWILSL ETALQKAQKG TRTNGAASSS
AHETAIQVHY DRNQPLTTIL LANKPLSKEG SEKDTRHYIF DLKNTGLHYE SGDALGVWPT
NAPALVEEVL EAVKLSPTEF VSVKDFGELP LSLALAKHYD ITRITPSILQ AVHERTNNDV
LSRLLRKENQ EELKQWLWGR QLADLLQEFP FPIQAAELVQ LLKPLQPRLY SISSSSKMNP
DEVHITVSTV RYPFNGKQRN GLCSTFLADH AEKAAGVPIF VQKTSHFRLP SDTDKPVIMV
GPGTGIGPFR GFLQERQATG AKGKNWLIFG EQRAECDFYY KKELEAMQQR GILHRLDTAF
SRDQAEKIYV QHRMIEHGAE LWSWLQAGAY FYVCGDASKM AKDVDTALKQ VIEQHGGKSA
AEAEQYVKAM AKEQRYARDV Y
//
