NARC_HALMT
ID NARC_HALMT Reviewed; 485 AA.
AC I3R9N1; Q703H8;
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=Probable respiratory nitrate reductase subunit cytochrome b-561;
GN Name=narC; OrderedLocusNames=HFX_5106; ORFNames=C439_00680;
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], AND IDENTIFICATION.
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 PUTATIVE REACTION MECHANISM, AND SUBUNIT.
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. Proposed
CC membrane-embedded heme-iron subunit involved in a protonmotive Q-cycle
CC mechanism-based electron transfer to the beta subunit.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups per subunit. {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}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Proposed to confer antimycin sensitivity to the
CC respiratory nitrate reductase.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
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DR EMBL; AJ621878; CAF21904.1; -; Genomic_DNA.
DR EMBL; CP001870; AFK20941.1; -; Genomic_DNA.
DR EMBL; AOLO01000001; EMA05269.1; -; Genomic_DNA.
DR RefSeq; WP_004056328.1; NZ_CP039141.1.
DR AlphaFoldDB; I3R9N1; -.
DR SMR; I3R9N1; -.
DR EnsemblBacteria; AFK20941; AFK20941; HFX_5106.
DR EnsemblBacteria; EMA05269; EMA05269; C439_00680.
DR GeneID; 40158242; -.
DR KEGG; hme:HFX_5106; -.
DR HOGENOM; CLU_031114_2_0_2; -.
DR OMA; WNYGPYD; -.
DR OrthoDB; 14275at2157; -.
DR Proteomes; UP000006469; Plasmid pHM300.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF13631; Cytochrom_B_N_2; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Nitrate assimilation; Plasmid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..485
FT /note="Probable respiratory nitrate reductase subunit
FT cytochrome b-561"
FT /id="PRO_0000428888"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 244..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 254..258
FT /note="KGGQP -> EGWTA (in Ref. 1; CAF21904)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="M -> V (in Ref. 1; CAF21904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 52699 MW; 1DDD08F8315B94DA CRC64;
MSRIDRLADQ SADAGNRVYD WMNARFDLDS GRKFLGKAFP AEDSFLLGEV ALFCFLLLVL
TGMFLGMFFE PSTSDVKYEG SVAKFQGEEV PEAFASVLHI TYDIPFGMFI RRMHHWAAHL
FVASIGLHML RVFFTGAYRN PREPNWVVGT ALAGLSMGAA YTGYALPFDE FAATATGIGY
NLATSIPLVG EVIGKAFFGG EFPSSATIPR LYFIHVLIIP IAIGVLLAIH MMILVRQKHT
EAPRDDDVRG LTPKGGQPTD GAVTSDGGTE SVVPKEDDSV VVGLPAFPNQ TAVSAVVFFL
TLATVAMLAG FLPVHNIAEY GPNNPAGTPE LIMPDWFLMW VYGLLKLLPS WMSFTIPVVG
IHISTEFVGG VLLPTLVFGI IAVWPFVDYH DKSVHFTANP LDRSWQTAVG VAAVQFIMIA
SIAGMNNLLG RALGVGTGVI NPILTVALFV VPIGSGLLTY RILEDSTEQE HARQYTEQAE
EADDD
