ID J4JVV7_9MYCO Unreviewed; 1413 AA.
AC J4JVV7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=FdhF {ECO:0000313|EMBL:EJO89707.1};
GN ORFNames=MCOL_V205940 {ECO:0000313|EMBL:EJO89707.1};
OS Mycobacterium colombiense CECT 3035.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1041522 {ECO:0000313|EMBL:EJO89707.1, ECO:0000313|Proteomes:UP000006455};
RN [1] {ECO:0000313|EMBL:EJO89707.1, ECO:0000313|Proteomes:UP000006455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 3035 {ECO:0000313|EMBL:EJO89707.1,
RC ECO:0000313|Proteomes:UP000006455};
RX PubMed=21952541; DOI=10.1128/JB.05928-11;
RA Gonzalez-Perez M., Murcia M.I., Landsman D., Jordan I.K.,
RA Marino-Ramirez L.;
RT "Genome sequence of the Mycobacterium colombiense type strain, CECT 3035.";
RL J. Bacteriol. 193:5866-5867(2011).
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:EJO89707.1}.
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DR EMBL; AFVW02000002; EJO89707.1; -; Genomic_DNA.
DR RefSeq; WP_007770341.1; NZ_CP020821.1.
DR STRING; 1041522.GCA_002105755_01889; -.
DR GeneID; 31526594; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0369; Bacteria.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000006455; 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 Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 4..66
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 866..1004
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1046..1262
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 830..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1413 AA; 153219 MW; 14A820F2A5B998B2 CRC64;
MAPENAVNTM CAYCGVGCGM VLQITTDPKT GRDHVAKSVG NKQHPANFGR LCTKGATTAD
MLAAPGRMDS AHARADRGEP LEPIDMDRAI SQCAKRLRAI IDEHGPDAFA MYVSGQMSIE
AQYLANKLTK GFVGTNQIES NSRLCMASAG SGYKLSLGAD GPPGSYQDFE HADVFFVIGA
NMADCHPILF LRMMDRVKAG AKLIVVDPRR TATADKADLF LQIAPGSDLA LLNGLLHLIV
ENGHTDADFI AEFTEGWEVM PSFLEQYTPD TVSAVTGIPE QDIRAAAQMI GEAGNFMSCW
TMGLNQSTHG TWNTNAICNL HLATGAICKP GSGPFSLTGQ PNAMGGREMG YMGPGLPGQR
SVASDDDRAF VENLWGIPRG TLRTEVGSGT IDMFSRMADG QIKACWIICT NPVASVANRK
TVLAGLERAE LVMAQDAFLE TETNEYADVL LPATLWTESE GVMVNSERNM TLFQPAVRAP
SHALPDWQII ARIACEMGFS EAFSYNCAEE VFEEIKRFSN PKTGYDLRGV SYERLRQGPL
QWPCAPEGDG DRNPIRYLND GVSQTQLVRE DGSVPRLAFP TATGRAVFFA RPHLLPEEMP
DDDYPFLLNT GRLPHQWHTM TKTGKVAKLN KLNPGPFVEI HPDDAARLQV SDDDQVEIAS
RRGRAVLPAL VSDRVRPGNC FAPFHWNDSF GEYLSINAVT NDAVDPISSQ PEFKACAVTL
TKIAVAEPVS GAETPAPTDT PEPAPTEVRE ISVSQVDALG ELLGVATQPK PEFNELGRSY
LAGMLSGLRS EAGRRAGGVP TLPLSAPFDS STRLWVDGLL AGLFSRIDGP QPVGMPEGSQ
PTPLTAAGQP PTAPADAKPA AERAPIVVLW ASQTGNAEEL AAEIAAQLGA AELPVTLQSM
DDFPVGELAA TKELLFVTST TGDGEAPDNG AGLWRALTGE GAPRFIDTRY AVLALGDSNY
DDFCGHGRKL DARLAELGAT RIADRVDCEP DYDDSAAKWV GGVIDALTKT PTSVGGDGAA
VAPVRTSPVA APSHQNGHAT SAYSKKHPLI TGMVRNTVLS QPESAKDVRH LVFDLPEDSV
TYEAGDALGV WPRNSDELVD EWLSVTGLNG QTPVEVGEHG LMSLRSALTE RIEIAHISRD
LVRFVQERTG DPTLAELLKP ENKRALADWT WGRQSIDLLS KLPVSASAHE WLRVLKRLQP
RLYSISSSPK ACPGEVHLTV SPVRFNFQGV PRRGVCSTYL ADRSPGDRVA VYLQQSSNFR
PPSDSDTPMI MIGPGTGIAP FRGFLQERRA LGHTGPNWLF FGEQHAATDF YYRDELEQMR
DDGFLTELDL AFSRDQQQKV YVQHLMRNRG AQLWSWLQDG AQLYVCGTAD PMAKDVDRAL
CEIAAEFGKL EPEAARDYVQ SLSADKRYHR DVY
//