ID A0A1E3SJ28_9MYCO Unreviewed; 1401 AA.
AC A0A1E3SJ28;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Reductase {ECO:0000313|EMBL:ODR02121.1};
GN ORFNames=BHQ21_22830 {ECO:0000313|EMBL:ODR02121.1};
OS Mycobacterium sherrisii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=243061 {ECO:0000313|EMBL:ODR02121.1, ECO:0000313|Proteomes:UP000094224};
RN [1] {ECO:0000313|Proteomes:UP000094224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1_M4 {ECO:0000313|Proteomes:UP000094224};
RA Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL Submitted (SEP-2016) 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:ODR02121.1}.
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DR EMBL; MIHC01000052; ODR02121.1; -; Genomic_DNA.
DR STRING; 243061.AWC25_12335; -.
DR Proteomes; UP000094224; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; 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.
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:UP000094224};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 857..995
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1034..1250
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 833..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1401 AA; 152234 MW; CFA6542FDACCD827 CRC64;
MCAYCGVGCG MVLQITTDPE SDRRHVAKCV GNKSHPANFG RLCTKGTTTA DMLAAPGRLD
SAYWRSERGA SLEQIDLDAA LTQSAKQLRA IIDEHGPDAF ALYVSGQMSL EAQYLANKLT
KGFIRTNQIE SNSRLCMASA GSGYKLSLGA DGPPGSYQDF DRADVFFVIG ANMADCHPIL
FLRMMDRVKA GAKLIVVDPR RTATAEKADL FLQISSGTDL ALLNGLLQQI VENGHTDPEF
IAEFTEGWEE MPGFLKHFTP ERVSDLTGIP EADIRTAARW IGEAENFMTC WTMGLNQSTH
GTWNTNAICN LHLATGAICK PGSGPFSLTG QPNAMGGREM GYMGPGLPGQ RAVTSAADRE
FVEDQWGIPR GSLRTDVGTG TVDMFSRMAK GEIKACWIIC TNPVASVANR KTVLAGLDRA
ELVIAQDAFF ETETNEYADV LLPAALWTEA EGVMINSERN MTLFQPAVGP PGQAMPDWQI
IARIACEMGY SESFTYSSAE EVFEEIKRFW NPKTGYDLRG ATYERLRRTP LQWPCPPECA
DDRNPIRYLN DGVSQAQLVR ADGSVPRLVF PTASGRAVFF ARPHLSPDEM PDDDYPFLLN
TGRLPHQWHT MTKTGKVAKL NKLNPGPFVE IHPDDAARLD VADGDKVEIA SRRGRAVLPA
VVTDRVRPGN CFAPFHWNDA FGEYLSINAV TNDAVDPVSY QPEFKACAVT VTKVAVATPE
VTADPEPSVA VDAAAPATSE VTEISVSQVD ALAEILGVAN EPAPQLGPLG RSYLAGVLAG
LRSEAGRRAA GVPTLPLNAP LDINTRLWVD GLLAGMFART DAPAAVPAIT SAVSTAEAPA
DPPKTPAAED DSKRGPIVVL WASQTGNAEE LAATIAARLA DAALSVKLHS MDDFPVADLP
ATRELLVITS TTGDGEAPDN GATLWRALSG EGAPRLGDTR YALLALGDSN YNDFCGYGRK
LDERLAELGA TRIAKRVDCE PDYEEAAAGW TDQVIKALTR TPSRVGPGTA APPAPATTAP
RPPAPAAAPA FNKKRPLVTD MIRNTTLSGP SSAKDVRQIV FDLPEEEVSY EAGDALGVWP
RNSDQLVDEW LAVTGLDGQT PVEVGEHGLM SLRTALTERI EIAHISRDVV RFVQERTGDR
TLARLLQPEN KTELNNWTWG RQSVDLLARL PVAASAHEWL RVLKRLQPRL YSISSSPKEC
PGEVHLTVSP VRYNFQGVPR RGVCSTYLAD RSPGDRVAVY LQPSSNFRIP SDAQTPMIMI
GPGTGIAPFR GFLQERRALG HTGPNWLFFG EQHAATDFYY REEIQAMHAD GLLTEMDLAF
SRDQAQKVYV QHLMRKRGAQ LWSWLQDGAH LYVCGTADPM AKDVDRALCE IAAEHGKLDP
DAARAYVQSL SADKRYHRDV Y
//