ID Q3JM03_BURP1 Unreviewed; 1398 AA.
AC Q3JM03;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=FdhF {ECO:0000313|EMBL:ABA52871.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:ABA52871.1};
DE EC=1.8.1.2 {ECO:0000313|EMBL:ABA52871.1};
GN Name=fdhF {ECO:0000313|EMBL:ABA52871.1};
GN OrderedLocusNames=BURPS1710b_A0241 {ECO:0000313|EMBL:ABA52871.1};
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA52871.1, ECO:0000313|Proteomes:UP000002700};
RN [1] {ECO:0000313|EMBL:ABA52871.1, ECO:0000313|Proteomes:UP000002700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b {ECO:0000313|EMBL:ABA52871.1,
RC ECO:0000313|Proteomes:UP000002700};
RA Woods D.E., Nierman W.C.;
RL Submitted (SEP-2005) 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}.
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DR EMBL; CP000125; ABA52871.1; -; Genomic_DNA.
DR RefSeq; WP_004528540.1; NC_007435.1.
DR EnsemblBacteria; ABA52871; ABA52871; BURPS1710b_A0241.
DR KEGG; bpm:BURPS1710b_A0241; -.
DR HOGENOM; CLU_000422_6_0_4; -.
DR Proteomes; UP000002700; Chromosome II.
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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABA52871.1}; 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 864..1002
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1030..1247
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 723..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 150260 MW; EBF89C98DF236F2D CRC64;
MTSASVKTVC PYCGVGCGMV LHVEDGEVVK VSGDAEHPTN LGRLCTKGSS AHVALRNAGR
LERAFVRDAR ELDPAPVPIA DAIAETARRL RATLDAHGPD ALAFYVSGQM SLEAQYLVNK
LAKGYVRTPH IESNSRLCMA SAGSGYKLSL GADGPPGSYQ DFERADLFFV IGSNMADCHP
ILFLRMMERV KAGAKLVVVD PRRTATAQKA DLFLKIRPGT DLALLNGLLH LLHANGRTDA
DFIAAHTEGW DAMPGFLADY TPQRVAALTG LAEADIRLAA QWIGDAREWT SCWTMGLNQS
THGTWNTNAI CNLHLATGKI CRPGSGPFSL TGQPNAMGGR EMGYMGPGLP GQRSALDGDD
RRFVEEIWGL PAGTIRPDAG GGTVDLFARM AAGDVKACWI ICTNPVATVA NRKNVIAGLQ
AADVVIVQDA FLDTETNRYA DILLPGALWA EAEGVMINSE RNLTLMRQAL EPPGDAWPDW
RIVAAVARGM GYGDAFDYGS AAEVFDEIRR FANPNTGYDL RGASHAALRA TPLQWPCPPE
DGRDRHPIRY LNDGASRPRV TLPDGRVPPL AFPTPSGKAR FFARPHVAPA EMPTPEFPIV
LNTGRLQHQW HTMTKTGKVA MLNKLDARPF VEIHPDDAAA LSIAANDAVE IRSARGRAVL
PAVVTDRVQP GACFAPMHWN DVYGDDLCVN AVTNDAVDPV SLQPELKFCA VVLARVDAPD
SADAGAHAGA HAAPLHETGS REAQAQAAPR AHEAACADAA PEEHDMSDID TFAALLGVPA
ATSAPQLTDA QRVYVAGFVS GLRSAEGRRA GGVPMLPASA PFDAKARLWL DGLLAGLFSR
APLGAADAVS APSGVRIVRT RPKVVLLWAS QTGNVESLTE RYATQLMDSG FEIRVACMSD
YPAASLAKAQ YALLMTSTFG DGDAPDNGQA FWTALAAAGA PRADGLRYAV LAFGDRNYDP
FCGHGRRLDA RLAELGATRL VERVDCDAEF QPAADAWLER AIARIKEEDA ALHAVPADGM
IPSGAIPTKT RPAASRLVAN LRLNEPGAAK DTRCVSLSAD GAAIEYETGD ALGVWPTNCP
ELVDELLALT RLKPDAPVTV AGMGELRLAD ALAKHLDITR PHPDALAFVA SRSRAGDALA
RLLGDDRKTD LKHWLWGQQL ADVLHEFPLE LSAAELVGML KRLQPRLYSI ASSPSAHRGE
IHLTVSAVRY GNGRRQRKGV ASTFLADRAA DAPVPVFVQK SAHFRPPASG DAPIVMVGPG
TGIAPFRGFL HERRARGAKG RNWLFFGEQH ADTDFYYRDE LAQMRADGFL TRLDVAFSRD
QTEKVYVQDR MLEQGAALWA WLEEGAHFYV CGDASRMAKD VDAALKTIVA RHGGMTDEQA
ADYVARLAKD KRYARDVY
//
