NASA_HALMT
ID NASA_HALMT Reviewed; 708 AA.
AC I3R634; Q703N5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Assimilatory nitrate reductase {ECO:0000303|PubMed:11731152, ECO:0000303|PubMed:16182473};
DE EC=1.7.7.2 {ECO:0000269|PubMed:11731152};
GN Name=nasA {ECO:0000303|PubMed:16182473}; OrderedLocusNames=HFX_2002;
GN ORFNames=C439_11788;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, INDUCTION, AND PATHWAY.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=16182473; DOI=10.1016/j.gene.2005.07.011;
RA Lledo B., Marhuenda-Egea F.C., Martinez-Espinosa R.M., Bonete M.J.;
RT "Identification and transcriptional analysis of nitrate assimilation genes
RT in the halophilic archaeon Haloferax mediterranei.";
RL Gene 361:80-88(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=11731152; DOI=10.1016/s0378-1097(01)00431-1;
RA Martinez-Espinosa R.M., Marhuenda-Egea F.C., Bonete M.J.;
RT "Assimilatory nitrate reductase from the haloarchaeon Haloferax
RT mediterranei: purification and characterisation.";
RL FEMS Microbiol. Lett. 204:381-385(2001).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation. Catalyzes the reduction of nitrate to nitrite,
CC using ferredoxin as the electron donor. Can use reduced methyl viologen
CC but neither NADPH nor NADH as electron donors.
CC {ECO:0000269|PubMed:11731152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + nitrite + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) +
CC nitrate + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21828,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.7.7.2;
CC Evidence={ECO:0000269|PubMed:11731152};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:11731152};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250|UniProtKB:Q57366};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250|UniProtKB:Q57366};
CC -!- ACTIVITY REGULATION: Inhibited by cyanide and azide.
CC {ECO:0000269|PubMed:11731152}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.95 mM for nitrate {ECO:0000269|PubMed:11731152};
CC KM=0.066 mM for methyl viologen {ECO:0000269|PubMed:11731152};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:11731152};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius at 2.2 and 3.1 M NaCl, and
CC 60 degrees Celsius at 0.9 and 1.3 M NaCl.
CC {ECO:0000269|PubMed:11731152};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000305|PubMed:16182473}.
CC -!- SUBUNIT: Is probably a monomer (PubMed:16182473). Initially
CC characterized as a dimer of proteins with a MW of 105 and 50 kDa
CC (PubMed:11731152). {ECO:0000269|PubMed:11731152,
CC ECO:0000305|PubMed:16182473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Repressed by the presence of ammonium as nitrogen source.
CC {ECO:0000269|PubMed:16182473}.
CC -!- MISCELLANEOUS: Enzyme stability and activity depend upon the salt
CC concentration. {ECO:0000269|PubMed:11731152}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000305}.
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DR EMBL; AJ621498; CAF19042.1; -; Genomic_DNA.
DR EMBL; CP001868; AFK19694.1; -; Genomic_DNA.
DR EMBL; AOLO01000009; EMA00016.1; -; Genomic_DNA.
DR RefSeq; WP_004059340.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R634; -.
DR SMR; I3R634; -.
DR STRING; 523841.HFX_2002; -.
DR EnsemblBacteria; AFK19694; AFK19694; HFX_2002.
DR EnsemblBacteria; EMA00016; EMA00016; C439_11788.
DR GeneID; 40155088; -.
DR KEGG; hme:HFX_2002; -.
DR PATRIC; fig|523841.21.peg.2383; -.
DR eggNOG; arCOG01491; Archaea.
DR OMA; GMNAHQH; -.
DR OrthoDB; 1029at2157; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0047889; F:ferredoxin-nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..708
FT /note="Assimilatory nitrate reductase"
FT /id="PRO_0000428892"
FT DOMAIN 15..73
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT REGION 586..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT CONFLICT 200
FT /note="A -> R (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="L -> I (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..352
FT /note="SSKGTW -> PRKNV (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="T -> S (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="A -> P (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="P -> R (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="T -> R (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
FT CONFLICT 612..617
FT /note="VNPETV -> STPRPS (in Ref. 1; CAF19042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 75211 MW; B8F054A1B6D7A525 CRC64;
MPRNLRFLSV VNHVTKQVPT TCMRCAVGCG HVHLGSENAY GLETVRGDPS HPVNNGLACG
RGIRESADPA GEWLTRPLVR EDGELVQTSW SDAMARVGAT IRTAVATDPD EVAVLGSGQQ
TNEAAYALGK LARAGIGTRN YDANTTLCMA SAVTAYYRAF GSDAPPPTYD DIPNAETHLV
WGANPAVAHP VMFRWIRQSA TDGRLVVVDP VETKTAAVAD DHVSVAPGGD LALARAILRH
LVDTDQIDES FVRSNTEGFD DVVSALPSVT DAAARAGVSL DTVEELAALL DAPTLIYWGM
GVNQSVRGTA TAGALVNLCL ASGNLGPGTG PFSLTGQANS MGTRVCSSKG TWSGHRPFEH
PDHRRAVAEA WDVPVSRLPD DSGPGPVGIL DSSPSVVWTV ATNPLAGFPD ATAAREVLRD
SFLVVQDAFR SDTVELADVV LPAATWGESE GTAMNMERTV SRIRAATETP PGVRQDLDII
ADVAARVAPG LLPRPPVSPS AIFDEFAALT EGTDADCSGI SYTRLDGERA VRWPAPEPNS
DAGYRYYDPS TSRWTFPTPS GKARFSTLDG EPLPEPVDGD YPLTLTTGRE ADGYNTGVRS
RSDTPEEPVA RVNPETVDTY HDAVADTDGE LRTTVVSRRA SVSVTLDRDD AVPPGLVWLS
IHHPMTNQLT SPAVDPQSNE PNFKQCAVRF VHPDAPAKAD FLAAEVSD
