NARX_MYCTO
ID NARX_MYCTO Reviewed; 652 AA.
AC P9WJQ0; L0T7S1; P71994; Q7D821;
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-like protein NarX;
GN Name=narX; OrderedLocusNames=MT1778;
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).
RN [2]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
CC -!- FUNCTION: Does not seem to have nitrate reductase activity.
CC {ECO:0000250|UniProtKB:P9WJQ1}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000305};
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000305};
CC Note=Binds 2 heme b groups per subunit. Heme 1 is located at the
CC cytoplasmic interface, heme 2 is located at the extracellular
CC interface. Electrons are transferred from the extracellular to the
CC cytoplasmic heme. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC {ECO:0000269|PubMed:12953092}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the nitrate reductase
CC alpha subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the NarJ/NarW family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the nitrate reductase
CC gamma subunit family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46051.1; -; Genomic_DNA.
DR PIR; C70688; C70688.
DR RefSeq; WP_003901238.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJQ0; -.
DR SMR; P9WJQ0; -.
DR PRIDE; P9WJQ0; -.
DR EnsemblBacteria; AAK46051; AAK46051; MT1778.
DR KEGG; mtc:MT1778; -.
DR PATRIC; fig|83331.31.peg.1908; -.
DR HOGENOM; CLU_027863_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR023234; NarG-like_domain.
DR InterPro; IPR036197; NarG-like_sf.
DR InterPro; IPR003816; Nitrate_red_gam.
DR InterPro; IPR003765; NO3_reductase_chaperone_NarJ.
DR InterPro; IPR036411; TorD-like_sf.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR Pfam; PF02665; Nitrate_red_gam; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF103501; SSF103501; 1.
DR SUPFAM; SSF89155; SSF89155; 1.
DR TIGRFAMs; TIGR00351; narI; 1.
DR TIGRFAMs; TIGR00684; narJ; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cell membrane; Electron transport; Heme; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..652
FT /note="Nitrate reductase-like protein NarX"
FT /id="PRO_0000427791"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 53..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT REGION 1..251
FT /note="Nitrate reductase alpha subunit"
FT REGION 258..415
FT /note="Nitrate reductase delta subunit"
FT REGION 416..652
FT /note="Nitrate reductase gamma subunit"
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 BINDING 469
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 602
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 620
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 652 AA; 72825 MW; E2D0513A9CB29F3E CRC64;
MTVTPRTGSR IEELLARSGR FFIPGEISAD LRTVTRRGGR DGDVFYRDRW SHDKVVRSTH
GVNCTGSCSW KIYVKDDIIT WETQETDYPS VGPDRPEYEP RGCPRGAAFS WYTYSPTRVR
HPYARGVLVE MYREAKARLG DPVAAWADIQ ADPRRRRRYQ RARGKGGLVR VSWAEATEMI
AAAHVHTIST YGPDRVAGFS PIPAMSMVSH AAGSRFVELI GGVMTSFYDW YADLPVASPQ
VFGDQTDVPE SGDWWDVVWQ CASVLLTYPN SRQLGTAEEL LAHIDGPAAD LLGRTVSELR
RADPLTAATR YVDTFDLRGR ATLYLTYWTA GDTRNRGREM LAFAQTYRST DVAPPRGETP
DFLPVVLEFA ATVDPEAGRR LLSGYRVPIA ALCNALTEAA LPYAHTVAAV CRTGDMMGEL
FWTVVPYVTM TIVAVGSWWR YRYDKFGWTT RSSQLYESRL LRIASPMFHF GILVVIVGHG
IGLVIPQSWT QAAGLSEGAY HVQAVVLGSI AGITTLAGVT LLIYRRRTRG PVFMATTVND
KVMYLVLVAA IVAGLGATAL GSGVVGEAYN YRETVSVWFR SVWVLQPRGD LMAEAPLYYQ
IHVLIGLALF ALWPFTRLVH AFSAPIGYLF RPYIIYRSRE ELVLTRPRRR GW
