NARG_MYCTU
ID NARG_MYCTU Reviewed; 1232 AA.
AC P9WJQ3; 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 47.
DE RecName: Full=Nitrate reductase alpha subunit;
DE EC=1.7.5.1;
GN Name=narG; OrderedLocusNames=Rv1161;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14645286; DOI=10.1128/jb.185.24.7247-7256.2003;
RA Sohaskey C.D., Wayne L.G.;
RT "Role of narK2X and narGHJI in hypoxic upregulation of nitrate reduction by
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 185:7247-7256(2003).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: The alpha chain is the actual site of nitrate reduction
CC (Probable). Supports anaerobic growth of E.coli on glycerol in an
CC E.coli mutant lacking endogenous nitrate reductase.
CC {ECO:0000269|PubMed:14645286, ECO:0000305}.
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 -!- ACTIVITY REGULATION: Increased nitrate reductase activity is seen under
CC hypoxic conditions, however this seems to be due to induction of the
CC probable nitrate/nitrite transporter narK2 rather than increased enzyme
CC activity.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- INDUCTION: Constitutively expressed; independent of nitrate and nitrate
CC levels. {ECO:0000269|PubMed:14645286}.
CC -!- DISRUPTION PHENOTYPE: Loss of nitrate reductase activity in aerobic and
CC hypoxic conditions. {ECO:0000269|PubMed:14645286}.
CC -!- MISCELLANEOUS: One of the activities induced in M.tuberculosis by
CC hypoxia is the dissimilatory reduction of nitrate to nitrite, which
CC serves to provide energy as the bacteria adapt to anaerobiosis.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43917.1; -; Genomic_DNA.
DR PIR; B70556; B70556.
DR RefSeq; NP_215677.1; NC_000962.3.
DR RefSeq; WP_003898748.1; NZ_NVQJ01000025.1.
DR AlphaFoldDB; P9WJQ3; -.
DR SMR; P9WJQ3; -.
DR STRING; 83332.Rv1161; -.
DR iPTMnet; P9WJQ3; -.
DR PaxDb; P9WJQ3; -.
DR GeneID; 885573; -.
DR KEGG; mtu:Rv1161; -.
DR TubercuList; Rv1161; -.
DR eggNOG; COG5013; Bacteria.
DR OMA; DKPSQYF; -.
DR PhylomeDB; P9WJQ3; -.
DR BRENDA; 1.7.5.1; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IGI:UniProtKB.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR GO; GO:0036294; P:cellular response to decreased oxygen levels; IGI:UniProtKB.
DR GO; GO:0071249; P:cellular response to nitrate; IGI:UniProtKB.
DR GO; GO:0071732; P:cellular response to nitric oxide; IGI:UniProtKB.
DR GO; GO:0042128; P:nitrate assimilation; IMP:MTBBASE.
DR GO; GO:0043602; P:nitrate catabolic process; IMP:MTBBASE.
DR GO; GO:0042126; P:nitrate metabolic process; IGI:UniProtKB.
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 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Cell membrane; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..1232
FT /note="Nitrate reductase alpha subunit"
FT /id="PRO_0000393357"
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"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
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
