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Database: UniProt
Entry: A0A2A7MTV3_MYCAG
LinkDB: A0A2A7MTV3_MYCAG
Original site: A0A2A7MTV3_MYCAG 
ID   A0A2A7MTV3_MYCAG        Unreviewed;      1233 AA.
AC   A0A2A7MTV3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE            EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN   ORFNames=CQY20_22470 {ECO:0000313|EMBL:PEG35242.1}, MAGR_47960
GN   {ECO:0000313|EMBL:GFG53355.1};
OS   Mycolicibacterium agri (Mycobacterium agri).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=36811 {ECO:0000313|EMBL:PEG35242.1, ECO:0000313|Proteomes:UP000220914};
RN   [1] {ECO:0000313|EMBL:PEG35242.1, ECO:0000313|Proteomes:UP000220914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG37673 {ECO:0000313|EMBL:PEG35242.1,
RC   ECO:0000313|Proteomes:UP000220914};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GFG53355.1, ECO:0000313|Proteomes:UP000465302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG53355.1,
RC   ECO:0000313|Proteomes:UP000465302};
RX   PubMed=31287781;
RA   Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA   Iida T., Fujita J., Nakamura S.;
RT   "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT   species based on 7547 genomic profiles.";
RL   Emerg. Microbes Infect. 8:1043-1053(2019).
RN   [3] {ECO:0000313|EMBL:GFG53355.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG53355.1};
RA   Matsumoto Y., Motooka D., Nakamura S.;
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC         Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC         ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001854};
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:PEG35242.1}.
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DR   EMBL; BLKS01000001; GFG53355.1; -; Genomic_DNA.
DR   EMBL; PDCP01000048; PEG35242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A7MTV3; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000220914; Unassembled WGS sequence.
DR   Proteomes; UP000465302; Unassembled WGS sequence.
DR   GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 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:0008940; F:nitrate reductase activity; IEA:InterPro.
DR   GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR   CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR   CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR   Gene3D; 3.40.50.12440; -; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR006468; NarG.
DR   NCBIfam; TIGR01580; narG; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220914}.
FT   DOMAIN          53..117
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1233 AA;  136007 MW;  99BFD2BD483227E4 CRC64;
     MTSPARIGGP IEELLERSGR FFTPGEFSAD LRTVTRRGGR DGDVFYRDRW SHDKVVRSTH
     GVNCTGSCSW KIYVKDGIIT WETQETDYPS VGPDRPEYEP RGCPRGAAFS WYTYSPTRVR
     YPYARGLLVE MYREAKARLG DPVLAWADIQ SGPERRRRYQ RARGKGGLVR VSWAEATEMI
     AAAHVHTIKT YGPDRVAGFS PIPAMSMVSH AAGSRFVELI GGAMTSFYDW YADLPVASPQ
     VFGDQTDVPE SGDWWDATYL MMWGSNVPVT RTPDAHWMVE VRYRGTKVVS VSPDYADNTK
     FADEWMPCAA GADGALAMAM GHVILSECFV HQRVPFFVDY VRSYTDLPFL VKLEQRDGAL
     VPGKNLTAAD LGHTTENAAF KPVLLDGKTD DVAVPHGSLG FRFGDDGVGK WNLDLGGLTP
     ALTVARHEAG GETALIQLPR FDTADGHGEV LARGVPVRRV GEHLVCTVFD LMLAHYGVAR
     PGLPGDWPTG YDDATHPYTP AWQEPITGVA AAQAERIAKE FARNAEESGG RSMIIMGAGI
     CQWFHGDATY RAVLALLLLT GSMGRNGGGW AHYVGQEKCR PVTGWATMAM ATDWSRPPRQ
     MAGTSYWYAH TDQWRYDGYR ADALASPLGR GRFRNKHTMD VLASAAAMGW SPFYPQFDRS
     SLDVADEALA AGRDKSEIGA YVAEQLASGK LKLAVTDPDD PANWPRVLNI WRANLLGSSS
     KGNEYFLRHL LGTDSNLQAK PTAEGLRPND VTWRDEIPEG KLDLLMSIDF RMTSTTLLSD
     VVLPAATWYE KADLSSTDMH PYVHAFTPAI DPPWETHSDF EAFGAIARAF SALAKNHLGV
     RTDIVVGALQ HDTPQAMAYP HGSENDWRTS AAVPVPGKTM GPVAVVERDY TAIADKWATL
     GPLVEQLGVT TKAVTTHPER EVGELAAKFG VAKSGPAQGR PAITTDERMA DVILALSGTS
     NGRLAVEGFR ELEKRTGRHL VHLAEGSEER RITYADAAAR PVPVITSPEW SGSETGGRRY
     APFTVNIEEL KPFHTLTGRM HFYLDHDWLE ELGEQLPTYR PPLDMQRLFG EPQVGDARDG
     IGLTVRYLTP HSKWSIHSEY QDNLLMLSLS RGGPTMWMSP ADAAKIDVRD NDWVEAVNRN
     GVLVCRAIVS HRMPEGVVFV YHVQERTIDV PLSETTGLRG GIHNTLTRLL IKPSHLAGGY
     AQNAFAFNYL GPTGNQRDEV TVVRRRSQEV TYQ
//
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