ID A0A0G2EPT4_9EURO Unreviewed; 479 AA.
AC A0A0G2EPT4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Acyl-CoA desaturase {ECO:0000256|PIRNR:PIRNR000345};
DE EC=1.14.19.1 {ECO:0000256|PIRNR:PIRNR000345};
GN ORFNames=UCRPC4_g02607 {ECO:0000313|EMBL:KKY24141.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY24141.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY24141.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY24141.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY24141.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY24141.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates. {ECO:0000256|PIRNR:PIRNR000345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, 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:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000345};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRNR:PIRNR000345};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR000345};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|PIRNR:PIRNR000345}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY24141.1}.
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DR EMBL; LCWF01000063; KKY24141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EPT4; -.
DR OrthoDB; 637961at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR009160; Acyl-CoA_deSatase_haem/ster-bd.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF000345; OLE1; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00075; FACDDSATRASE.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|PIRNR:PIRNR000345};
KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000345};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000345};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000345};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000345};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR000345}.
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 353..431
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 54103 MW; E909CD44CE2ED759 CRC64;
MSSQPTAGHL AVKPEYLSSQ PSPMAKASEP NRSKSYDPKK PHITETPITK YNWYKHVNWL
NVTLIVLIPL YGCIGAFWTP LQLKTAIFAV LYYFATGLGI TAGYHRLWAH TSYSATLPLR
IFLAALGGGA VEGSVRWWAR DHRAHHRYTD TDKDPYSVRK GLLYSHIGWM LMKQNPKRIG
RTDISDLNED PVVVWQHKNY LKVVLFMGLV FPTLVAGICW GDFLGGFVYG GILRIFFVQQ
ATFCVNSLAH WLGDQPFDDR NSPRDHVLTA LVTLGEGYHN FHHEFPSDYR NAIEWFQYDP
TKWFIWTMKQ VGLAYDLKQF RANEIEKGRI QQMQKKLDQE RAKLDWGVPL DQLPVMEWDD
YVDQAKNGRG LIAVAGVVHD VSDFIKDHPG GKAMIKSGIG KDATAMFNGG VYLHSNAAHN
LLSTMRVGVI RGGCEVEIWK KSQAQENGKI VRDENGNRIV RAGEQVTKAM QNMPVAGAA
//
