CARF_MYXXA
ID CARF_MYXXA Reviewed; 281 AA.
AC Q9AE87;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Plasmanylethanolamine desaturase {ECO:0000303|PubMed:31604315};
DE EC=1.14.19.77 {ECO:0000269|PubMed:31604315};
DE AltName: Full=Carotenogenesis protein CarF {ECO:0000303|PubMed:12519205};
DE Short=CarF {ECO:0000303|PubMed:12519205};
GN Name=carF {ECO:0000303|PubMed:12519205};
OS Myxococcus xanthus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP AND MUTAGENESIS OF HIS-78; HIS-103; HIS-113 AND HIS-218.
RC STRAIN=DK1050;
RX PubMed=12519205; DOI=10.1046/j.1365-2958.2003.03319.x;
RA Fontes M., Galbis-Martinez L., Murillo F.J.;
RT "A novel regulatory gene for light-induced carotenoid synthesis in the
RT bacterium Myxococcus xanthus.";
RL Mol. Microbiol. 47:561-571(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hartzell P.L., Youderian P.A.;
RT "Identification of genes required for adventurous gliding motility in
RT Myxococcus xanthus with the transposable element mariner.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CARR, DOMAIN, MUTAGENESIS
RP OF HIS-78; HIS-103; HIS-113; HIS-164; HIS-195 AND HIS-218, AND TOPOLOGY.
RC STRAIN=DK1050;
RX PubMed=18310035; DOI=10.1099/mic.0.2007/013359-0;
RA Galbis-Martinez L., Galbis-Martinez M., Murillo F.J., Fontes M.;
RT "An anti-antisigma factor in the response of the bacterium Myxococcus
RT xanthus to blue light.";
RL Microbiology 154:895-904(2008).
RN [4]
RP FUNCTION, AND DOMAIN.
RC STRAIN=DK1050;
RX PubMed=22267513; DOI=10.1128/jb.06662-11;
RA Galbis-Martinez M., Padmanabhan S., Murillo F.J., Elias-Arnanz M.;
RT "CarF mediates signaling by singlet oxygen, generated via photoexcited
RT protoporphyrin IX, in Myxococcus xanthus light-induced carotenogenesis.";
RL J. Bacteriol. 194:1427-1436(2012).
RN [5]
RP FUNCTION, DOMAIN, MUTAGENESIS OF HIS-78; HIS-103; HIS-104; HIS-113;
RP HIS-164; HIS-168; HIS-183; HIS-190; HIS-191; HIS-194; HIS-195 AND HIS-218,
RP AND CATALYTIC ACTIVITY.
RX PubMed=31604315; DOI=10.1126/science.aay1436;
RA Gallego-Garcia A., Monera-Girona A.J., Pajares-Martinez E.,
RA Bastida-Martinez E., Perez-Castano R., Iniesta A.A., Fontes M.,
RA Padmanabhan S., Elias-Arnanz M.;
RT "A bacterial light response reveals an orphan desaturase for human
RT plasmalogen synthesis.";
RL Science 366:128-132(2019).
CC -!- FUNCTION: Plasmanylethanolamine desaturase involved in plasmalogen
CC biogenesis in the membrane, required for light-induced carotenogenesis
CC (PubMed:12519205, PubMed:18310035, PubMed:22267513, PubMed:31604315).
CC Plasmalogens are glycerophospholipids with a hydrocarbon chain linked
CC by a vinyl ether bond at the glycerol sn-1 position, and are involved
CC in antioxidative and signaling mechanisms, most precisely in sensing
CC photooxidative stress through singlet oxygen (PubMed:31604315).
CC Participates in the light-dependent inactivation of the antisigma
CC factor CarR (PubMed:12519205, PubMed:18310035). Mediates signaling by
CC singlet oxygen, generated via photoexcited protoporphyrin IX
CC (PubMed:22267513). {ECO:0000269|PubMed:12519205,
CC ECO:0000269|PubMed:18310035, ECO:0000269|PubMed:22267513,
CC ECO:0000269|PubMed:31604315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1,2-saturated alkyl)-2-acyl-sn-glycero-3-
CC phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1-O-
CC (1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:22956, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:75028, ChEBI:CHEBI:77290; EC=1.14.19.77;
CC Evidence={ECO:0000269|PubMed:31604315};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22957;
CC Evidence={ECO:0000269|PubMed:31604315};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(13-methyltetradecyl)-2-(13-methyltetradecanoyl)-sn-
CC glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = 1-O-(1Z-13-methyltetradecenyl)-2-(13-methyltetradecanoyl)-sn-
CC glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:61972, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145179,
CC ChEBI:CHEBI:145180; Evidence={ECO:0000269|PubMed:31604315};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61973;
CC Evidence={ECO:0000269|PubMed:31604315};
CC -!- SUBUNIT: Interacts with CarR. {ECO:0000269|PubMed:18310035}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:18310035}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Histidine box-1 and -2 together with other histidine residues
CC are essential for catalytic activity. {ECO:0000269|PubMed:12519205,
CC ECO:0000269|PubMed:18310035, ECO:0000269|PubMed:22267513,
CC ECO:0000269|PubMed:31604315}.
CC -!- DISRUPTION PHENOTYPE: Deletion prevents the activation of the light
CC inducible promoters of carQ, crtI and carB.
CC {ECO:0000269|PubMed:12519205}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase CarF family.
CC {ECO:0000305}.
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DR EMBL; AY204462; AAO22861.1; -; Genomic_DNA.
DR EMBL; AJ311657; CAC34626.1; -; Genomic_DNA.
DR RefSeq; WP_011555701.1; NZ_JABFNQ010000107.1.
DR AlphaFoldDB; Q9AE87; -.
DR SwissLipids; SLP:000001974; -.
DR GeneID; 41362993; -.
DR OMA; RTQECIC; -.
DR BioCyc; MetaCyc:MON-21879; -.
DR BRENDA; 1.14.19.77; 3551.
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:0050207; F:plasmanylethanolamine desaturase activity; IDA:UniProtKB.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR019547; Lipid_desat.
DR Pfam; PF10520; Lipid_desat; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..281
FT /note="Plasmanylethanolamine desaturase"
FT /id="PRO_0000448849"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18310035"
FT TRANSMEM 29..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..58
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18310035"
FT TRANSMEM 59..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18310035"
FT TRANSMEM 124..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..142
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18310035"
FT TRANSMEM 143..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18310035"
FT MOTIF 164..168
FT /note="Histidine box-1"
FT /evidence="ECO:0000269|PubMed:31604315"
FT MOTIF 191..195
FT /note="Histidine box-2"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 78
FT /note="Essential for plasmanylethanolamine desaturase
FT activity"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 103
FT /note="Essential for plasmanylethanolamine desaturase
FT activity"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 104
FT /note="Essential for plasmanylethanolamine desaturase
FT activity"
FT /evidence="ECO:0000269|PubMed:31604315"
FT SITE 113
FT /note="Essential for plasmanylethanolamine desaturase
FT activity"
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 78
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:12519205,
FT ECO:0000269|PubMed:18310035, ECO:0000269|PubMed:31604315"
FT MUTAGEN 103
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:12519205,
FT ECO:0000269|PubMed:18310035, ECO:0000269|PubMed:31604315"
FT MUTAGEN 104
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 113
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:12519205,
FT ECO:0000269|PubMed:18310035, ECO:0000269|PubMed:31604315"
FT MUTAGEN 164
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:18310035,
FT ECO:0000269|PubMed:31604315"
FT MUTAGEN 168
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 183
FT /note="H->A: No effect on plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 190
FT /note="H->A: No effect on plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 191
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 194
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:31604315"
FT MUTAGEN 195
FT /note="H->A: Impaired carotenoid synthesis caused by loss
FT of plasmanylethanolamine desaturase activity."
FT /evidence="ECO:0000269|PubMed:18310035,
FT ECO:0000269|PubMed:31604315"
FT MUTAGEN 218
FT /note="H->A: No effect on plasmanylethanolamine desaturase
FT activity."
FT /evidence="ECO:0000269|PubMed:12519205,
FT ECO:0000269|PubMed:18310035, ECO:0000269|PubMed:31604315"
SQ SEQUENCE 281 AA; 31210 MW; 02D4597978D29A0A CRC64;
MKTQEIEKKV RQQDAQVLAQ GYSPAIRAME IAAIVSFVSL EVALVYRLWG TPYAGTWLLL
SAVLLGYLAA DFVSGFVHWM GDTWGSTEMP VLGKALIRPF REHHVDEKAI TRHDFVETNG
NNCLISLPVA IIALCLPMSG PGWVFCASFL GAMIFWVMAT NQFHKWSHMD SPPALVGFLQ
RVHLILPPDH HRIHHTKPYN KYYCITVGWM NKPLTMVHFF PTAERLITWA TGLLPRQDDI
GAEAARALVV AAGGSEAPVV QAAKELLTQA TVQEKPASTR P
