NASD_HALMT
ID NASD_HALMT Reviewed; 586 AA.
AC I3R637; Q703N2;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Assimilatory ferredoxin-dependent nitrite reductase {ECO:0000303|PubMed:16182473};
DE Short=NiR {ECO:0000303|PubMed:16182473};
DE EC=1.7.7.1 {ECO:0000269|PubMed:11267765};
DE AltName: Full=Ferredoxin:nitrite reductase {ECO:0000305};
GN Name=nasD {ECO:0000303|PubMed:16182473};
GN Synonyms=fdx-niR {ECO:0000312|EMBL:CAF19045.1}; OrderedLocusNames=HFX_2005;
GN ORFNames=C439_11803;
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], FUNCTION, 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, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11267765; DOI=10.1111/j.1574-6968.2001.tb10550.x;
RA Martinez-Espinosa R.M., Marhuenda-Egea F.C., Bonete M.J.;
RT "Purification and characterisation of a possible assimilatory nitrite
RT reductase from the halophile archaeon Haloferax mediterranei.";
RL FEMS Microbiol. Lett. 196:113-118(2001).
CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonium in the nitrate
CC assimilation pathway, using ferredoxin as the electron donor. Can use
CC reduced methyl viologen but neither NADPH nor NADH as electron donors.
CC {ECO:0000269|PubMed:11267765}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) +
CC nitrite + 6 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:18041,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.7.7.1;
CC Evidence={ECO:0000269|PubMed:11267765};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000269|PubMed:11267765};
CC Note=Binds 1 siroheme per subunit. {ECO:0000250|UniProtKB:P9WJ03};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:11267765};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by cyanide and azide.
CC {ECO:0000269|PubMed:11267765}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.6 mM for nitrite {ECO:0000269|PubMed:11267765};
CC KM=1.9 mM for methyl viologen {ECO:0000269|PubMed:11267765};
CC Vmax=4.1 umol/min/mg enzyme with nitrite as substrate
CC {ECO:0000269|PubMed:11267765};
CC Vmax=1.7 umol/min/mg enzyme with methyl viologen as substrate
CC {ECO:0000269|PubMed:11267765};
CC Note=In the presence of 3.2 M NaCl.;
CC pH dependence:
CC Optimum pH is 7.5 at 60 degrees Celsius. At 40 degrees Celsius
CC (temperature of the natural environment for H.mediterranei) the
CC optimum pH is 6.5. {ECO:0000269|PubMed:11267765};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:11267765};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000305|PubMed:16182473}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11267765}.
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:11267765}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; AJ621501; CAF19045.1; -; Genomic_DNA.
DR EMBL; CP001868; AFK19697.1; -; Genomic_DNA.
DR EMBL; AOLO01000009; EMA00019.1; -; Genomic_DNA.
DR RefSeq; WP_004059343.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R637; -.
DR SMR; I3R637; -.
DR STRING; 523841.HFX_2005; -.
DR EnsemblBacteria; AFK19697; AFK19697; HFX_2005.
DR EnsemblBacteria; EMA00019; EMA00019; C439_11803.
DR GeneID; 40155085; -.
DR KEGG; hme:HFX_2005; -.
DR eggNOG; arCOG02055; Archaea.
DR HOGENOM; CLU_015667_2_3_2; -.
DR OMA; IKISGCM; -.
DR OrthoDB; 4523at2157; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0048307; F:ferredoxin-nitrite reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:CACAO.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.413.10; -; 2.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; SSF55124; 2.
DR SUPFAM; SSF56014; SSF56014; 2.
DR PROSITE; PS00365; NIR_SIR; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Electron transport; Heme; Iron; Iron-sulfur; Metal-binding;
KW Nitrate assimilation; Oxidoreductase; Transport.
FT CHAIN 1..586
FT /note="Assimilatory ferredoxin-dependent nitrite reductase"
FT /id="PRO_0000428891"
FT REGION 566..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 411
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WJ03"
FT BINDING 417
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WJ03"
FT BINDING 455
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WJ03"
FT BINDING 459
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WJ03"
FT BINDING 459
FT /ligand="siroheme"
FT /ligand_id="ChEBI:CHEBI:60052"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P9WJ03"
FT CONFLICT 175
FT /note="D -> N (in Ref. 1; CAF19045)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..217
FT /note="LEPARKEVDGEVI -> WNPPGKRSTERLF (in Ref. 1;
FT CAF19045)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="K -> Q (in Ref. 1; CAF19045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 65438 MW; DCA1E981EE4B5210 CRC64;
MASKKEQWKS DLYGDAVRDE LEAFAEEGFE SIPEDERDKW FTRFKFWGVF QQRTGQESYF
MMRLTNANGV LEPGQLRTIA EVARDYATGP VDNPEFGNGW VDLTTRQSIQ LHWLELEDIP
EIWEQLESVG VTSRSAGGDT MRNITGCPVA GKDTHELVES KPLLDRFQSE LREDDALSNM
PRKFNISVTG CREGCAQDSI NDIGLEPARK EVDGEVITGF NVRVGGGLGS RKPRVARSLD
VFVADEERAY EVVRGFVELY HDHGNRDVRA RARSRFFVDD WGTEKIRDRL ESEYLDFELQ
SAGEDIRDEY TYNAGRPQSA GKSDHVGVHE QSDGRYYVGL SVAVGRLTAA DALELADLAD
KYGSGKIRLT RRQNPIVMDV PAGALDDLLA EPLLSKHTPE PNPFQRGTVA CTGTEFCSLA
LTETKARTAR MLRWLRDNVE VPDDVHQLKI HYSGCTADCG QANTADIGLF GMRAQKDGEM
VEAMDIGVGG GIGDEPSFVE WIHQRVPADE VPGAIASLVE AFAAHRTAGQ TFRQWVEAEG
PDAVAEYCEP IETDFEAPYM HDAKQSWYPF ADEDEPPKTE QPMTSD
