DESAT_THAPS
ID DESAT_THAPS Reviewed; 515 AA.
AC Q4G2T3; B8C381;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Sphingolipid 10-desaturase;
DE EC=1.14.19.19 {ECO:0000269|PubMed:23510654};
DE AltName: Full=Fatty acid desaturase A {ECO:0000303|PubMed:15978045};
DE Short=TpdesA {ECO:0000303|PubMed:15978045};
GN Name=desA {ECO:0000312|EMBL:AAX14503.1};
GN ORFNames=THAPS_22804 {ECO:0000312|EMBL:EED92516.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15978045; DOI=10.1111/j.1742-4658.2005.04755.x;
RA Tonon T., Sayanova O., Michaelson L.V., Qing R., Harvey D., Larson T.R.,
RA Li Y., Napier J.A., Graham I.A.;
RT "Fatty acid desaturases from the microalga Thalassiosira pseudonana.";
RL FEBS J. 272:3401-3412(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23510654; DOI=10.1016/j.phytochem.2013.02.010;
RA Michaelson L.V., Markham J.E., Zaeeuner S., Matsumoto M., Chen M.,
RA Cahoon E.B., Napier J.A.;
RT "Identification of a cytochrome b5-fusion desaturase responsible for the
RT synthesis of triunsaturated sphingolipid long chain bases in the marine
RT diatom Thalassiosira pseudonana.";
RL Phytochemistry 90:50-55(2013).
CC -!- FUNCTION: Fatty acid desaturase that catalyzes the introduction of the
CC third double bond at the Delta(10) position in d18:3Delta4,8,10
CC triunsaturated sphingolipid long fatty acid chains. The cytochrome b5
CC domain probably acts as the direct electron donor to the active site of
CC the desaturase. {ECO:0000269|PubMed:23510654}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (4E,8E)-4-sphinga-4,8-dienine ceramide + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = 2 Fe(III)-[cytochrome b5] + 2 H2O +
CC N-acyl-(4E,8E,10E)-sphingatrienine; Xref=Rhea:RHEA:46548, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:85953, ChEBI:CHEBI:86294;
CC EC=1.14.19.19; Evidence={ECO:0000269|PubMed:23510654};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305}.
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; AY817153; AAX14503.1; -; mRNA.
DR EMBL; CM000642; EED92516.1; -; Genomic_DNA.
DR RefSeq; XP_002290764.1; XM_002290728.1.
DR AlphaFoldDB; Q4G2T3; -.
DR SMR; Q4G2T3; -.
DR EnsemblProtists; EED92516; EED92516; THAPSDRAFT_22804.
DR GeneID; 7448146; -.
DR KEGG; tps:THAPSDRAFT_22804; -.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_016265_1_1_1; -.
DR BioCyc; MetaCyc:MON-19157; -.
DR BRENDA; 1.14.19.19; 6253.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000001449; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; 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; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IDA:UniProtKB.
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; IPR018506; Cyt_B5_heme-BS.
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 SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="Sphingolipid 10-desaturase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004238894"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 46..113
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 245..249
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 281..286
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 447..451
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 90
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 113
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 CONFLICT 470
FT /note="T -> R (in Ref. 1; AAX14503)"
SQ SEQUENCE 515 AA; 58957 MW; 69EC2E379FE10093 CRC64;
MRAVWALLWA LQLGTLVGCA LVLGVHHFSG DNLTKQSAIP TKSSKAKPIS DQKAAVTSGS
TCAVREKARK DGLVLLDGNW YNVEKFVHHH PGGVEVLEQY LGADISFVFR VMHRNPTQIM
KYRKPVRAAT PEELEALTSR RQEVCLDMMD DFVTNSIDIA SPEMLPKPTQ FDLKSFEKDF
IDLYEEFVAQ GYFKPSTTWL LWNTAVLISI IALSVISMKV LPPTSFVLPG ALLGLFWHQS
GFLMHDAEHH NLAGNERLND ILGWIYGTVF LGVNGAWWRE EHREHHAFLN TYDDESGFKD
PQMREDVWIQ NKKLIPFFGD EIIHFLTNFQ HILFLPIIFI VGRVGIVVDS TLTERKFRPW
TILGNVCHIL LHYAILSQTS RPIPVYIIGS LWQAILSLQL LGNHYVKPWN RLNDATEGNF
CVWQILSTQD FACPRWSRWL YGGLNFHYSH HLFPTLSREY FHITSPRIRT LCEKHGLPFI
EIAFIDCVVG MVNNFNEVRK DFATKGHGSV AFMYT
