ID L0IXQ1_9MYCO Unreviewed; 1355 AA.
AC L0IXQ1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Sulfite reductase, alpha subunit (Flavoprotein) {ECO:0000313|EMBL:AGB24095.1};
DE EC=1.8.1.2 {ECO:0000313|EMBL:AGB24095.1};
GN ORFNames=Mycsm_03826 {ECO:0000313|EMBL:AGB24095.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB24095.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) 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; CP003078; AGB24095.1; -; Genomic_DNA.
DR STRING; 212767.Mycsm_03826; -.
DR KEGG; msa:Mycsm_03826; -.
DR PATRIC; fig|710686.3.peg.3860; -.
DR HOGENOM; CLU_000422_6_2_11; -.
DR Proteomes; UP000010844; Chromosome.
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:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:AGB24095.1}; Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 25..85
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 824..958
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 991..1229
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1355 AA; 148224 MW; E424D2417C2DD451 CRC64;
MSTSFHCDNV AAKEHETLLD HHCFVAVTRT ACSYCGVGCG IEVQTAEKDG KTVIARVSGD
KLHPTNFGRL CTKGATHAEM MAADDGRLKS ALLRPTRADE PVPTPVDDAV AEAGRRLRAI
IDEHGPDAVA LYVSGQMSIE AQYLAAKLAK GFIQTVHIES NSRLCMASAG AGFKQSLGAD
GPPGSYTDFD CTDLFFVIGS NMADCHPILY LRMADRLKAG ARLIVVDPRR TTTAEHADLF
LQIKAGTDLA LLNGILHLLV ENGDIDTEFI AEHTEGWDAM PAFLADYPPD RVAEITGLAE
SDIRTAARMI ADAGEWMSCW TMGLNQSTHG TWNTNAICNL HLATGAICRP GSGPMSLTGQ
PNAMGGREMG YMGPGLPGQR SVLSADDRAF VETQWGLEPG TIRSDVGPGT IDMFEQLADG
TIKACWIICT NPVATVANRK TVITGLENAH LVITQDAYAT TATNNYADIV LPATLWAESD
AVMVNSERNL TLLQQSIPPA GQSRPDWQLI CQVAAHMGFG EHFDYQSSEQ IFDEIRRFAN
PKTGYDLRGA SYERLRQTPL QWPCPPDDAD RHPIRYLNDG VSQDLFVDEN DDTPRLAFPT
PSRRAVFHAR PHMDARELPD EDFPLVLNTG RLQHQWHTMT KTGKVDKLNK LDSGPFVEIH
PVDAAALDIV AGQPVELTSR RGRAVLPAVV TDRVRPGNCF VPFHWNDEHG EYLTINALTN
DAVDPDSLQP EFKVCAVGLR PVKTMDPVVD ELDLSQRKPT LTEGEKIYLA AFFSGLAEGV
SGVPVLPASA PVATGVRLWI DGLLAGRYSR LTTTPELQPT KAGPLVLWAS QTGNAEDFAA
RLAERLGDSQ LVNMDDMQLA ELAAARDVLV ITSTFGDGGP PDNGAGFWDR LHAADAPALD
GVRYAVLGIG DRSYANFCGH AKAIDGRLSA LGATRMLDRT ECEVYDNEPM DRWAERITAL
VAETVAKPPN GHNGGVPTVT KPKRAEPFTR AKPLLAPLSR NTVLTAPTSR KEVRQFGFDI
SEYDVSYAVG DSLGVYATND PATVDAWLTA TGLSGDTSVE VDGNEQSLRD ALIVSYDICR
VTPNLLRFVA ESCRDKAAAK ALMAPKDKLD KWLVDRNGLD IVQEFAVRAE PEEWQEVLVR
LTPRNYSISS SPLISSNEVQ VTVSVVRYRG ADGGQRGGVC STFLADRAAA APVFLQRSPH
FRPPEDGGTP MIMVGPGTGV APFRGFLQER RALGHGGRNW LFFGDRYRSE NFYYRDDFED
MVRDGFLNRL DLAFSRDQAK RVYVQHKMLD YGADVWRWLD DGAHFYVCGD ANRMARDVDA
ALTSIIKTHG SMSDEDAHDY KRELVASKRY VRDVY
//
