ID E3KD58_PUCGT Unreviewed; 591 AA.
AC E3KD58;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN ORFNames=PGTG_07693 {ECO:0000313|EMBL:EFP82296.2};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP82296.2, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
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DR EMBL; DS178281; EFP82296.2; -; Genomic_DNA.
DR RefSeq; XP_003326715.2; XM_003326667.2.
DR AlphaFoldDB; E3KD58; -.
DR STRING; 418459.E3KD58; -.
DR EnsemblFungi; EFP82296; EFP82296; PGTG_07693.
DR GeneID; 10529669; -.
DR KEGG; pgr:PGTG_07693; -.
DR VEuPathDB; FungiDB:PGTG_07693; -.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_016265_3_1_1; -.
DR InParanoid; E3KD58; -.
DR OrthoDB; 294339at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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:SF30; DELTA 8-(E)-SPHINGOLIPID DESATURASE; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 2.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 400..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..95
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 591 AA; 67643 MW; A461B89340399330 CRC64;
MANNPGLLVD QLSKDPVDSV PFLTRNQIKT SIALGQVLVL HRSYVYKLNA WLNKHPGGEL
AILHFVGRDA TDEIEAYHPE KVIKQMRPFI VGKVVPEEWE DKKAGVGWKP LNPPIQIGLW
PMPCTDEIHP EPLRKKPEPI LRKSDHLAIL DHTLDHNSRS IPDSSKNFRT IDHVTSSTRL
DEVLSALEPA PDPPQEAFQE GYDLSPARQK HLSNSYRVLH DKIRAAGLYR APQPFYGYGP
DLLRYSVLFL AFFLTHPAFP LLKRYLASFL LDPTDVPFVE TPSTLRCFVS AVFLGLWWHQ
ITFVAHDAGH SGITGDWLKD RLIGILIGNF LGGISIGWWC DNHDVHHLVT NHPEHDPDIQ
HLPFFAISTK FFKSLRSTYY KHTMRFNRFA KFSVKHQHQF YYFIMLFARF NLLFNSCLYL
ATRKKQKMRN LEIAGIIFFW VYFGFILSLL PGIPTRIMFL LVSFAVTSPL HVQIVLSHFA
QSTADLGLNE CFAHRQIRTT MDVSCPPWLD FLHGGLHMQV THHLFPRLPR HRLRLASERF
VQPWCRQEGL TYSSMGFVQG NSKVLGTLQE VGKQLKILGT VASAQAHGLK H
//
