ID G8RXQ8_MYCRN Unreviewed; 1258 AA.
AC G8RXQ8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Sulfite reductase, alpha subunit (Flavoprotein) {ECO:0000313|EMBL:AEV75671.1};
GN OrderedLocusNames=MycrhN_5196 {ECO:0000313|EMBL:AEV75671.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV75671.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV75671.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV75671.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003169; AEV75671.1; -; Genomic_DNA.
DR RefSeq; WP_014213412.1; NC_016604.1.
DR AlphaFoldDB; G8RXQ8; -.
DR STRING; 710685.MycrhN_5196; -.
DR KEGG; mrh:MycrhN_5196; -.
DR PATRIC; fig|710685.3.peg.5217; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_000422_6_2_11; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000005442; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 1..62
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 743..876
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 897..1126
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1258 AA; 137777 MW; 70895DF861ED17BF CRC64;
MVTRTACSYC GVGCGIEVHS AVNSDTGRPV IARVTGDKLH PTNFGRLCTK GATHAEMMAA
VNGRLSTALV RTARGEEPVP ILVDDAVAEA GRRLRAIVDE HGPDAVALYV SGQMSIEAQY
LATKLAKGFL RTVHIESNSR LCMASAGTGF KQSLGADGPP GSYTDFDCSD LFFVIGSNMA
DCHPILYLRM ADRLKAGAKL IVVDPRRTAT AERADLFLQI RPGTDLALLN GLLHLLLEDE
ANNGAIDFDF IAEHTEGWDS MPAFLADYTP EVVAQLTGLA EEDIRTAARM IAEAGEWMSC
WTMGLNQSTH GTWNTNAICN LHLATGAICR PGSGPMSLTG QPNAMGGREM GYMGPGLPGQ
RSVVSAADRE FVEQQWALEP GTIRPDVGPG TIDMFGQLAD GRIKACWIIC TNPVATVANR
KTVIAGLEAA ELVITQDAYS ATATNRYADI VLPATLWAES DAVMVNSERN LTLLAQSIPP
HGDSRPDWQL ICQVAAHLGY GEHFDYESSE QIFDEIRRFS NPKTGYDLRG VSYARLRETS
LQWPCPPDDE NDRHPIRYLN DGVSQDHFVD ENGHMPRLAF PTPSRRAVFH ARPHMDAREL
PDDDYPFVLN TGRLQHQWHT MTKTGKVDTL NKLNGRPFVE IHPLDAAALD ISDDQPVELT
TRRGRAVLPA VVSDRVREGT CFVPFHWNDE DGEYLAVNAL TNDAVDPDSL QPEFKACAVT
LRPVGAAVRA NAALTRPDLT DGPLVLWASQ TGRAEEFAGK VAAAIGAPNL VNMNDLALAE
LAARDVLIVT STFGDGGPPD NGAEFWKRLN SPNAPTLTGM RFAVLGIGDR TYDNFCGHAK
MLDARLAALG AARLLDRVEC EAYDDAPMGR WVDQAAALLG RSVSSKPAPV AEPFTRAHPI
VAPLVRNVVL TTGASRKEVR QFGFDVSEHD VDYAAGDSLG VCPTNDPATV DAWLAATGMR
GQHVVEVDGV EQTLRDALMS RYDICRITPD LLRFIADHSR DAKALRAPKH KLDRWLAGRD
GLDLVQEFVV HADPVEWLDV LVRLTPRNYS ISSSPLVSPN EIQLTVSVVR YHGADGRRRG
GVCSTFLADR AASAPVFLQR SPHFRPPADS GTPMIMVGPG TGIAPFRGFL QERRALGHAG
RNWLFFGDQH RNENFYYRHD LEDMARDGFL SRLDLAFSRD QSDRVYVQHK MLDRGADVWR
WLDDGGHFYV CGDATRMAKD VDAALTTIIE THGRMSREGA HDFKRELVAA KRYVRDVY
//
