ID   NARG_MYCTO              Reviewed;        1232 AA.
AC   P9WJQ2; L0T628; O06559; Q7D8Q9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Nitrate reductase alpha subunit;
DE            EC=1.7.5.1;
GN   Name=narG; OrderedLocusNames=MT1198;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: The alpha chain is the actual site of nitrate reduction.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45455.1; -; Genomic_DNA.
DR   PIR; B70556; B70556.
DR   RefSeq; WP_003898748.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJQ2; -.
DR   SMR; P9WJQ2; -.
DR   EnsemblBacteria; AAK45455; AAK45455; MT1198.
DR   KEGG; mtc:MT1198; -.
DR   PATRIC; fig|83331.31.peg.1298; -.
DR   HOGENOM; CLU_000422_14_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
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:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 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   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR01580; narG; 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; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Transport.
FT   CHAIN           1..1232
FT                   /note="Nitrate reductase alpha subunit"
FT                   /id="PRO_0000427790"
FT   DOMAIN          53..117
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         60
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         64
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         68
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         103
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         233
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1232 AA;  136956 MW;  F12194DA383644F9 CRC64;
     MTVTPHVGGP LEELLERSGR FFTPGEFSAD LRTVTRRGGR EGDVFYRDRW SHDKVVRSTH
     GVNCTGSCSW KIYVKDGIIT WETQQTDYPS VGPDRPEYEP RGCPRGASFS WYSYSPTRVR
     YPYARGVLVE MYREAKTRLG DPVLAWADIQ ADPERRRRYQ QARGKGGLVR VSWAEASEMV
     AAAHVHTIKT YGPDRVAGFS PIPAMSMVSH AAGSRFVELI GGVMTSFYDW YADLPVASPQ
     VFGDQTDVPE SGDWWDASYL VMWGSNVPIT RTPDAHWMAE ARYRGAKVVV VSPDYADNTK
     FADEWVRCAA GTDTALAMAM GHVILSECYV RNQVPFFVDY VRRYTDLPFL IKLEKRGDLL
     VPGKFLTAAD IGEESENAAF KPALLDELTN TVVVPQGSLG FRFGEDGVGK WNLDLGSVVP
     ALSVEMDKAV NGDRSAELVT LPSFDTIDGH GETVSRGVPV RRAGKHLVCT VFDLMLAHYG
     VARAGLPGEW PTGYHDRTQQ NTPAWQESIT GVPAAQAIRF AKEFARNATE SGGRSMIIMG
     GGICHWFHSD VMYRSVLALL MLTGSMGRNG GGWAHYVGQE KVRPLTGWQT MAMATDWSRP
     PRQVPGASYW YAHTDQWRYD GYGADKLASP VGRGRFAGKH TMDLLTSATA MGWSPFYPQF
     DRSSLDVADE ARAAGRDVGD YVAEQLAQHK LKLSITDPDN PVNWPRVLTV WRANLIGSSG
     KGGEYFLRHL LGTDSNVQSD PPTDGVHPRD VVWDSDIPEG KLDLIMSIDF RMTSTTLVSD
     VVLPAATWYE KSDLSSTDMH PYVHSFSPAI DPPWETRSDF DAFAAIARAF SALAKRHLGT
     RTDVVLTALQ HDTPDEMAYP DGTERDWLAT GEVPVPGRTM SKLTVVERDY TAIYDKWLTL
     GPLIDQFGMT TKGYTVHPFR EVSELAANFG VMNSGVAVGR PAITTAKRMA DVILALSGTC
     NGRLAVEGFL ELEKRTGQRL AHLAEGSEER RITYADTQAR PVPVITSPEW SGSESGGRRY
     APFTINIEHL KPFHTLTGRM HFYLAHDWVE ELGEQLPVYR PPLDMARLFN QPELGPTDDG
     LGLTVRYLTP HSKWSFHSTY QDNLYMLSLS RGGPTMWMSP GDAAKINVRD NDWVEAVNAN
     GIYVCRAIVS HRMPEGVVFV YHVQERTVDT PRTETNGKRG GNHNALTRVR IKPSHLAGGY
     GQHAFAFNYL GPTGNQRDEV TVVRRRSQEV RY