NAR7_HALMT
ID NAR7_HALMT Reviewed; 276 AA.
AC I3R9M7; Q703H3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Putative respiratory nitrate reductase heme subunit ORF7;
GN OrderedLocusNames=HFX_5102; ORFNames=C439_00700;
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].
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 SUBUNIT, AND PUTATIVE REACTION 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. May
CC transfer electrons to the iron-sulfur centers of the catalytic beta
CC subunit.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250};
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:17888006}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein.
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DR EMBL; AJ621883; CAF21909.1; -; Genomic_DNA.
DR EMBL; CP001870; AFK20937.1; -; Genomic_DNA.
DR EMBL; AOLO01000001; EMA05273.1; -; Genomic_DNA.
DR RefSeq; WP_004056337.1; NZ_CP039141.1.
DR AlphaFoldDB; I3R9M7; -.
DR SMR; I3R9M7; -.
DR EnsemblBacteria; AFK20937; AFK20937; HFX_5102.
DR EnsemblBacteria; EMA05273; EMA05273; C439_00700.
DR GeneID; 40158238; -.
DR KEGG; hme:HFX_5102; -.
DR HOGENOM; CLU_982137_0_0_2; -.
DR OMA; PYICMGT; -.
DR OrthoDB; 66867at2157; -.
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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd09623; DOMON_EBDH; 1.
DR InterPro; IPR019020; Cyt-c552/DMSO_Rdtase_haem-bd.
DR InterPro; IPR017838; DMSO_Rdtase_II_haem_b-bd_su.
DR Pfam; PF09459; EB_dh; 2.
DR SMART; SM00887; EB_dh; 1.
DR TIGRFAMs; TIGR03477; DMSO_red_II_gam; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Nitrate assimilation; Plasmid; Transport.
FT CHAIN 1..276
FT /note="Putative respiratory nitrate reductase heme subunit
FT ORF7"
FT /id="PRO_0000428889"
FT BINDING 138
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 140..143
FT /note="STRN -> EHPY (in Ref. 1; CAF21909)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="T -> S (in Ref. 1; CAF21909)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..274
FT /note="AVQKNG -> RYRRRR (in Ref. 1; CAF21909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 29561 MW; F779E9FC0281F18E CRC64;
MSKKSEKRAT AVAAVVVCLV VLLTAVGPAM VTARPANEIP VESVLAEDQP QQPTSEAWNS
VPAVEVPMAS APSGLPNASD TSIETLRVQS ARTEERLYVR LSWADGTADR NISGPQQFVD
AAAVQVPVNT TARPPISMGS TRNPVNVWYW RADGETEELL AGGPGTTTKF EQSAVETKTA
YDDGRWTIVM SRELNSDAEN RTSFAANDDV DVAFAVWNGS QMERSGRKSV SEWYHFPFGP
GPQGPPYESI LWTVAGLAIV GVALVTIQAV QKNGGD
