NARG_HALMT
ID NARG_HALMT Reviewed; 984 AA.
AC I3R9M9; Q703H6;
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=Respiratory nitrate reductase subunit alpha;
DE EC=1.7.5.1 {ECO:0000269|PubMed:15342113};
DE AltName: Full=Nitrate reductase alpha chain;
DE Flags: Precursor;
GN Name=narG; OrderedLocusNames=HFX_5104; ORFNames=C439_00690;
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, ACTIVITY
RP REGULATION, SUBUNIT, INDUCTION, SUBCELLULAR LOCATION, AND
RP 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 alpha
CC chain is the actual site of nitrate reduction.
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; 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: Inhibited by cyanide, azide and antimycin A.
CC Enzyme stability is not dependent on salt concentration.
CC {ECO:0000269|PubMed:15342113, 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}.
CC -!- INDUCTION: By nitrate. {ECO:0000269|PubMed:15342113}.
CC -!- PTM: Exported by the Tat system. {ECO:0000269|PubMed:17888006}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ621880; CAF21906.1; -; Genomic_DNA.
DR EMBL; CP001870; AFK20939.1; -; Genomic_DNA.
DR EMBL; AOLO01000001; EMA05271.1; -; Genomic_DNA.
DR RefSeq; WP_004056332.1; NZ_CP039141.1.
DR AlphaFoldDB; I3R9M9; -.
DR SMR; I3R9M9; -.
DR PRIDE; I3R9M9; -.
DR EnsemblBacteria; AFK20939; AFK20939; HFX_5104.
DR EnsemblBacteria; EMA05271; EMA05271; C439_00690.
DR GeneID; 40158240; -.
DR KEGG; hme:HFX_5104; -.
DR HOGENOM; CLU_000422_13_3_2; -.
DR OMA; PFIHPFN; -.
DR OrthoDB; 1029at2157; -.
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: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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR03479; DMSO_red_II_alp; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Plasmid;
KW Signal; Transport.
FT SIGNAL 1..?
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN ?..984
FT /note="Respiratory nitrate reductase subunit alpha"
FT /id="PRO_0000428886"
FT DOMAIN 103..167
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 249
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 CONFLICT 281..282
FT /note="SN -> VE (in Ref. 1; CAF21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..434
FT /note="TTVQTQ -> QRSNP (in Ref. 1; CAF21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 564..566
FT /note="NTD -> TPN (in Ref. 1; CAF21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="W -> R (in Ref. 1; CAF21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="Q -> L (in Ref. 1; CAF21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="K -> R (in Ref. 1; CAF21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="P -> S (in Ref. 1; CAF21906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 984 AA; 111326 MW; 4CECDC63C15F628E CRC64;
MSRNDASQLD DGETTAESPP DDQANDAPEV GDPPGDPVDA DSGVSRRTFL EGIGVASLLG
IGTSAASDDS LFQMGGLKPV DDPIGNYPYR DWEDLYREKW DWDSVSRSTH SVNCTGSCSW
NVYVKNGQVW REEQSGDYPR FDESLPDPNP RGCQKGACYT DYVNADQRIK HPLKRVGERG
EGKWKRISWD EALTEIAEHV VDEVEAGRYD AISGFTPIPA MSPVSFASGS RLVNLLGGVS
HSFYDWYSDL PPGQPITWGT QTDNAESADW YNADYIIAWG SNINVTRIPD AKYFLESGYN
GTKRVGVFTD YSQTAIHTDE WLSPDSGTDT ALALGMAQTI VDEGLYDEAH LKEQTDMPLL
VRQDTGKFLR ASDVPSVNTD ADRPEWMLLM LDSNGRIREA PGSLGERDGQ KDYSKSIELD
FDPQLDGETT VQTQSGRVQV RTVWAELRDE LANWDPEMVH EETTVGKETY QRIAREFAEA
DKAKIIQGKG VNDWYHNDLG NRALQLLVTL TGNLGEQGTG LDHYVGQEKI WTFHGWKTLS
FPTGKVRGVP TTLWTYYHAG ILDNTDPDTA AKIRESIDKG WMPVYPEERD NGSRPDPTTM
FVWRGNYFNQ AKGNVAVEEQ LWPKLDLVVD INFRMDSTAM YSDIVLPTAS HYEKHDLSMT
DMHTYVHPFT PAVEPLGESK TDWQIFRELA QKIQEVATER GVEPISDRKF DREIDLQSVY
DDYVRDWETG EEGALAEDRA ACEYILEHSE ESNPADSDEQ ITFADTVEQP QRLLEAGDHW
TSDIEDGEAY APWKDFVQDK NPWPTVTGRQ QYYIDHDWFL ELGEELPTHK EGPENTGGDY
PMEYNTPHGR WAIHSTWRDS EKLLRLQRGE PLLYLHPEDA EERGIEDGDS VEVFNDLAEV
ELQAKIYPSS QRGTARMYFA WERFQFDSDS NFNSLVPMYM KPTQLVQYPE DSGEHLHFFP
NYWGPTGVNS DVRVDVRKAG GGDE
