ACET6_CERPU
ID ACET6_CERPU Reviewed; 483 AA.
AC Q9LEN0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Bifunctional delta 6-fatty acyl acetylenase/desaturase {ECO:0000303|PubMed:10848999};
DE Short=CpAcet6 {ECO:0000303|PubMed:10848999};
DE EC=1.14.19.38 {ECO:0000269|PubMed:10848999};
DE EC=1.14.19.47 {ECO:0000269|PubMed:10848999};
OS Ceratodon purpureus (Fire moss) (Dicranum purpureum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Dicranidae; Pseudoditrichales; Ditrichaceae;
OC Ceratodon.
OX NCBI_TaxID=3225 {ECO:0000312|EMBL:CAB94992.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=10848999; DOI=10.1046/j.1432-1327.2000.01418.x;
RA Sperling P., Lee M., Girke T., Zahringer U., Stymne S., Heinz E.;
RT "A bifunctional delta-fatty acyl acetylenase/desaturase from the moss
RT Ceratodon purpureus. A new member of the cytochrome b5 superfamily.";
RL Eur. J. Biochem. 267:3801-3811(2000).
CC -!- FUNCTION: Fatty acid acetylenase able to introduce a delta(6)-triple
CC bond into gamma-linolenic and stearidonic acid. Also able to introduce
CC a delta(6)-double bond into delta(9)-unsaturated fatty-acid substrates.
CC {ECO:0000269|PubMed:10848999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,12Z)-octadeca-9,12-dien-
CC 6-ynoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46536, 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:88242,
CC ChEBI:CHEBI:90081; EC=1.14.19.38;
CC Evidence={ECO:0000269|PubMed:10848999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,12Z,15Z)-octadeca-
CC 9,12,15-trien-6-ynoyl-containing glycerolipid + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:46540, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88244,
CC ChEBI:CHEBI:90079; EC=1.14.19.38;
CC Evidence={ECO:0000269|PubMed:10848999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-
CC octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:46288, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90078,
CC ChEBI:CHEBI:90079; EC=1.14.19.47;
CC Evidence={ECO:0000269|PubMed:10848999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-
CC containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46284, 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:88351,
CC ChEBI:CHEBI:90081; EC=1.14.19.47;
CC Evidence={ECO:0000269|PubMed:10848999};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:10848999}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AJ250734; CAB94992.1; -; mRNA.
DR AlphaFoldDB; Q9LEN0; -.
DR SMR; Q9LEN0; -.
DR KEGG; ag:CAB94992; -.
DR BioCyc; MetaCyc:MON-15862; -.
DR UniPathway; UPA00658; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102865; F:delta6-acyl-lipid desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..483
FT /note="Bifunctional delta 6-fatty acyl
FT acetylenase/desaturase"
FT /id="PRO_0000435458"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 60..134
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 212..216
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 249..253
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 421..425
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 95
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:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 117
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:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 483 AA; 54858 MW; C451D042169AB1C2 CRC64;
MALVTDFLNF LGTTWSKYSV YTHSYAGNYG PTLKHAKKVS AQGKTAGQTL RQRSVQDKKP
GTYSLADVAS HDRPGDCWMI VKEKVYDISR FADDHPGGTV ISTYFGRDGT DVFATFHPPA
AWKQLNDYYI GDLAREEPLD ELLKDYRDMR AEFVREGLFK SSKAWFLLQT LINAALFAAS
IATICYDKSY WAIVLSASLM GLFVQQCGWL AHDFLHQQVF ENRTANSFFG YLFGNCVLGF
SVSWWRTKHN IHHTAPNECD EQYTPLDEDI DTLPIIAWSK EILATVESKR ILRVLQYQHY
MILPLLFMAR YSWTFGSLLF TFNPDLSTTK GLIEKGTVAF HYAWFSWAAF HILPGVAKPL
AWMVATELVA GLLLGFVFTL SHNGKEVYNE SKDFVRAQVI TTRNTKRGWF NDWFTGGLDT
QIEHHLFPTM PRHNYPKIAP QVEALCKKHG LEYDNVSVVG ASVAVVKALK EIADEASIRL
HAH
