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Database: UniProt
Entry: A0A0H1B3R8_9EURO
LinkDB: A0A0H1B3R8_9EURO
Original site: A0A0H1B3R8_9EURO 
ID   A0A0H1B3R8_9EURO        Unreviewed;       409 AA.
AC   A0A0H1B3R8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000256|PIRNR:PIRNR017228};
DE            EC=1.14.19.17 {ECO:0000256|PIRNR:PIRNR017228};
GN   ORFNames=EMPG_10550 {ECO:0000313|EMBL:KLJ06025.1};
OS   Blastomyces silverae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ06025.1, ECO:0000313|Proteomes:UP000053573};
RN   [1] {ECO:0000313|Proteomes:UP000053573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- FUNCTION: Delta(4)-fatty-acid desaturase which introduces a double bond
CC       at the 4-position in the long-chain base (LCB) of ceramides.
CC       {ECO:0000256|PIRNR:PIRNR017228}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:46544, 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:31488,
CC         ChEBI:CHEBI:52639; EC=1.14.19.17;
CC         Evidence={ECO:0000256|PIRNR:PIRNR017228};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|PIRNR:PIRNR017228}.
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. DEGS
CC       subfamily. {ECO:0000256|ARBA:ARBA00006146,
CC       ECO:0000256|PIRNR:PIRNR017228}.
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:KLJ06025.1}.
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DR   EMBL; LDEV01003318; KLJ06025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H1B3R8; -.
DR   STRING; 2060906.A0A0H1B3R8; -.
DR   OrthoDB; 5485164at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000053573; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR   CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR   InterPro; IPR011388; DES1/DES2.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR   PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR   PANTHER; PTHR12879:SF8; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   Pfam; PF08557; Lipid_DES; 1.
DR   PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR   SMART; SM01269; Lipid_DES; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR017228};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017228};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR017228};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053573};
KW   Sphingolipid metabolism {ECO:0000256|PIRNR:PIRNR017228};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          35..73
FT                   /note="Sphingolipid delta4-desaturase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01269"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  45379 MW;  1BFB724338EA6D27 CRC64;
     MPSVVTTSSA RARVSTSAGK SSSSTRAPPP PSNSSVEDQF FWTYTEEPHR SRRQAIIKAH
     PEVTKLCGIE PLTKYVVLGV VSLQVACAYL LRNTPVLSWQ FLLTGYVIGA TSNQNLFLAI
     HEISHNLAFK SPFANRLLAI FANLPIGIPY SAAFRPYHLT HHKSLGVASL DTDLPTALEA
     FFLDSVLGKA FFCTFQILFY ALRPMFIYSP PFTSIHLLNI IVQFTFDYCL YKLCGSSLQP
     IYYLILSSFL AGSLHPCAGH FIAEHYFFSK TGAGTESIEE LRRQESGDKQ TIEKPTGDAL
     ANLPPPETYS YYGPLNILTY NVGLHNEHHD FPAVPWTRLH ALHNIAKEFY EPLPSHRSWV
     WVIYTFILDS NVGLWCRVKR AEGGRIVGGG GGVGGSGDGV GWKESEIQN
//
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