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Database: UniProt
Entry: A0A1E3SJ28_9MYCO
LinkDB: A0A1E3SJ28_9MYCO
Original site: A0A1E3SJ28_9MYCO 
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
//
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