NARH_HALMT
ID NARH_HALMT Reviewed; 352 AA.
AC I3R9M8; Q703H5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Respiratory nitrate reductase subunit beta;
DE EC=1.7.5.1 {ECO:0000269|PubMed:15342113};
DE AltName: Full=Nitrate reductase beta chain;
GN Name=narH; OrderedLocusNames=HFX_5103; ORFNames=C439_00695;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OG Plasmid pHM300.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP INDUCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=15342113; DOI=10.1016/j.bbagen.2004.05.007;
RA Lledo B., Martinez-Espinosa R.M., Marhuenda-Egea F.C., Bonete M.J.;
RT "Respiratory nitrate reductase from haloarchaeon Haloferax mediterranei:
RT biochemical and genetic analysis.";
RL Biochim. Biophys. Acta 1674:50-59(2004).
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 ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT, AND PUTATIVE REACTION
RP MECHANISM.
RX PubMed=17888006; DOI=10.1111/j.1574-6968.2007.00887.x;
RA Martinez-Espinosa R.M., Dridge E.J., Bonete M.J., Butt J.N., Butler C.S.,
RA Sargent F., Richardson D.J.;
RT "Look on the positive side! The orientation, identification and
RT bioenergetics of 'Archaeal' membrane-bound nitrate reductases.";
RL FEMS Microbiol. Lett. 276:129-139(2007).
CC -!- FUNCTION: The respiratory membrane-bound nitrate reductase enzyme
CC complex plays a role in generation of metabolic energy by using nitrate
CC as a terminal electron acceptor during anaerobic conditions. The beta
CC chain is an electron transfer unit containing four cysteine clusters
CC involved in the formation of iron-sulfur centers.
CC {ECO:0000269|PubMed:15342113}.
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 Evidence={ECO:0000269|PubMed:15342113};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P11349};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P11349};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:P11349};
CC Note=Binds 1 [3Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P11349};
CC -!- ACTIVITY REGULATION: Inhibited by cyanide, azide and antimycin A.
CC Enzyme stability is not dependent on salt concentration.
CC {ECO:0000269|PubMed:17888006}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.82 mM for nitrate {ECO:0000269|PubMed:15342113};
CC KM=0.25 mM for methyl viologen {ECO:0000269|PubMed:15342113};
CC Note=Characterized with purified enzyme corresponding to a dimer of
CC NarG and NarH.;
CC pH dependence:
CC Optimum pH is 8.2. At 40 degrees Celsius (temperature of natural
CC environment) the optimum pH is 7.9. {ECO:0000269|PubMed:15342113};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:15342113};
CC -!- SUBUNIT: Probable multiprotein complex; a catalytic heterodimer of an
CC alpha and beta chain is proposed to associate with additional subunits
CC involved in membrane attachment and electron transfer.
CC {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15342113,
CC ECO:0000305|PubMed:17888006}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006};
CC Extracellular side {ECO:0000269|PubMed:15342113,
CC ECO:0000269|PubMed:17888006}. Note=Proposed to be coexported with the
CC Tat system-dependent alpha subunit.
CC -!- INDUCTION: By nitrate. {ECO:0000269|PubMed:15342113}.
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DR EMBL; AJ621881; CAF21907.1; -; Genomic_DNA.
DR EMBL; CP001870; AFK20938.1; -; Genomic_DNA.
DR EMBL; AOLO01000001; EMA05272.1; -; Genomic_DNA.
DR RefSeq; WP_004056335.1; NZ_CP039141.1.
DR AlphaFoldDB; I3R9M8; -.
DR SMR; I3R9M8; -.
DR EnsemblBacteria; AFK20938; AFK20938; HFX_5103.
DR EnsemblBacteria; EMA05272; EMA05272; C439_00695.
DR GeneID; 40158239; -.
DR KEGG; hme:HFX_5103; -.
DR HOGENOM; CLU_043374_5_2_2; -.
DR OMA; NHCTHPS; -.
DR OrthoDB; 105930at2157; -.
DR BRENDA; 1.7.7.2; 2566.
DR BRENDA; 1.97.1.1; 2566.
DR Proteomes; UP000006469; Plasmid pHM300.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd10555; EBDH_beta; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017839; DMSO_Rdtase_II_Fe-S_su.
DR Pfam; PF13247; Fer4_11; 1.
DR TIGRFAMs; TIGR03478; DMSO_red_II_bet; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Nitrate assimilation; Oxidoreductase; Plasmid; Repeat;
KW Transport.
FT CHAIN 1..352
FT /note="Respiratory nitrate reductase subunit beta"
FT /id="PRO_0000428887"
FT DOMAIN 20..48
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 139..170
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 172..201
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 63..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 32
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 160
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 181
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 187
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 229
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 233
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT CONFLICT 132
FT /note="G -> C (in Ref. 1; CAF21907)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..160
FT /note="EAC -> GSL (in Ref. 1; CAF21907)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..315
FT /note="DT -> RH (in Ref. 1; CAF21907)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..324
FT /note="VN -> SH (in Ref. 1; CAF21907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40390 MW; C0A34119DE660316 CRC64;
MSTDSDAETV DLADGVDHQV AMVMDLNKCI GCQTCTVACK SLWTEGGGRD YMYWNNVETK
PGKGYPRNWE ESGGGWKSSE HKERKPGQIP DKEDYGDAWE FNHEEIMYNG SDRPLRPDSD
PEWGPNWDED QGTGEYPNSY YFYLPRICNH CTHPSCVEAC PRKAIYKREE DGIVLIDQER
CRGYRYCVEG CPYKKVYYNA TQKTSEKCIF CYPRIEGEGP DGKTFAPACA EDCPPQLRLV
GFLDDEQGPI HKLVEEYEVA LPLHPEYQTQ PNVYYIPPFA PPQHSEDGES VDVDRIPRNY
LEELFGERVH DALDTIERER EKVNRGGGSE LLDMLTDTNP ARKFRLEVFD DD
