ID F0WJB3_9STRA Unreviewed; 2058 AA.
AC F0WJB3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=3-dehydrosphinganine reductase {ECO:0000256|ARBA:ARBA00026112};
DE EC=1.1.1.102 {ECO:0000256|ARBA:ARBA00026112};
GN Name=AlNc14C120G6640 {ECO:0000313|EMBL:CCA21360.1};
GN ORFNames=ALNC14_075030 {ECO:0000313|EMBL:CCA21360.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA21360.1};
RN [1] {ECO:0000313|EMBL:CCA21360.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA21360.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH;
CC Xref=Rhea:RHEA:22640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:58299, ChEBI:CHEBI:58349;
CC EC=1.1.1.102; Evidence={ECO:0000256|ARBA:ARBA00024581};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
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DR EMBL; FR824165; CCA21360.1; -; Genomic_DNA.
DR EnsemblProtists; CCA21360; CCA21360; ALNC14_075030.
DR HOGENOM; CLU_240369_0_0_1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006666; P:3-keto-sphinganine metabolic process; IEA:InterPro.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd08939; KDSR-like_SDR_c; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR045022; KDSR-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43550; 3-KETODIHYDROSPHINGOSINE REDUCTASE; 1.
DR PANTHER; PTHR43550:SF3; 3-KETODIHYDROSPHINGOSINE REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF01363; FYVE; 2.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00064; FYVE; 2.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50178; ZF_FYVE; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT TRANSMEM 1734..1752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1876..1893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1899..1917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2021..2040
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..264
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 299..355
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 378..438
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1960..1979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 599..684
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2058 AA; 235687 MW; 3A347D3D64DD18A4 CRC64;
MSPNSDLAAT EADSTPATAG TNKVDTAMML DDITTNSDRV CSECDQKVAD TDDFCIFCGT
KVGSKLQDIS KQVLSSPTKD TSTKKPSEED TSILSKEAST TEEPVQKAFF DSNEEAPTVK
EPIEEMTKKE ETPPVVEPIK TTKATSPRST IASGPANNKP TADVEAGSLN LPRSSNSIDD
RFSTSFLGSS AASLEQLWVP DNFSSNCMDC KSPFGFPKPR RHHCRVCGLL FCRNCLQNKV
VVPKSFGYGE NKERCCRNCV TALQVKSISS PADVFNQRKS SHQIQSQANR QNSNHAVENQ
YEILGVTKNA SAKEIQNQFH SMSSSEKDQE VLTKLQDAYE TLQNPSKRQE HDTNIDRSQN
SMLGESCSFQ SNPTEMVRSD QTECQVCYRP FKFGRRQHHC RRCTRSVCNN CSEGMKPILE
LGFPQPVRHC STCMTKPPSF IQPVMDPVTK PPAGFEYLTR MDICVSVTQS KDEDMYEIKT
YCEPNEAILK EMKYTLTETE RAVANDYRIT HPRTLSDFEW LVTAMGNCTN IKALPFFPDR
RAIRNERDRG ASGYQGFIVG CLLHPLLRDS DCLKSFLVLP PKELTKYRSS SKPRPLYENE
KYENVITALR LEFERAQVRR RIDLLNSRKE AHEKRMEEQK ERLNQQRKRE AAQIVRRENA
TTRFRALEAR KESETERMER EKSRFLQQAE ATHILYFDKE QDAFVRNQEE ENLAKEKIEF
TKSKDMFQSD TTEWNTNMAL WSKHRANWSE HHNPAVSKDI ANEWILKFYG IYYSKVDNIN
GTEGIDAQVP PELVKLHAKM VELQEQEPGF LDEEGTAVDD EWSKLAKERE HWASDRANMK
REDEMCKDED VRYKQEHEYV SKEVEAREAK IAVVEKDMQM LQQQIHSRHK IIAQRLQRHQ
ALDQEFEKEW QVSLKNRTNG TKIRLGAHQT RISRTEKRCE LFLDQLQRQQ QSQRMLLFKR
ATLLEERSQD TQMFEEHQED SHVALEACQN ARALTPEYIN RMEADMKNRS EELKSVMESN
KPTSQEGGDL DERDGFMNKV RQQRTEYQNE LKQQLEALER EGKLCVSLLE RIQKYQAALD
EEIEDGAIED TLIANFVSLK SKEEKLLKEE EVLREEKKRS IQTLINDAGT WVLKAIHEHS
KRKKEEASRL VGQAQRAAEL QKLVQHFTHR VIDQEERIMR QKQRIINCEH KIEMLKAADN
WYEYVMEILS PDFGKKDGQK LEAGRIERME DLKEAARLQK EDESDMKKVA TLLEACKQYA
VSKEEKRAIW AKVEEVYSVT KAQEKEEDLM MTSQIRDLLQ QLGEAFEMLT NRLLEEEESL
QHASNQLEGE IESIKSFMER MEKEESTLGT AEKSSLAKES QVNRSESDLI KQRARTLIET
YKQMHNEHQN YPIKAEKIQQ RRSERPGPGA LRVSEMEAVK KIIKTRNYYD ARACGEFARK
FKIDQEMKEA RHVLDWFRKD LDQIIRDSEL WAEASRKDRK QIEGVKLKAA EMDWDHDTLS
KIPALLDVQK KLSDKKSNAS QSSDRRNANR TPGNQDGVSV HPDEQWLVEL IDLKRKISDL
DAIVLKNIGK MLHTAKQDEK AVVANLQQMK NDKEYILNTL RFIDQEEARA IRLAGKVSFP
SQRNLMGHEE SGSEEVETPR SIERSASSSK RFTPRSSKRD KTRQEASKSA KNPEETVKSQ
SEESVEPGKL PDPARRTSST AAASNYDYRL CFIGRIELSY NHNCVLSIRI FMELFWGFLL
CILALAALSF AWSKFKAPGF DVAGKHVFIT GGTSGLGLSL AKKYAIAGAK VSIIGRSTEK
LDNAKCDIEA VQKPGQPVVF STSCDVTKLK DVEDTISAAN RFHERATDYV ICNAGSAEPG
YFLAQDMSVF RRMMDLNYFG VVHTVKAALP AMIERDEPAH IVIVSSACAL ISFIGYTQYC
ASKYAVRGFA EALRSEMLLY KIKVHVFYPG SIDTPGFVEE NRTKPQETST IEGSSTLHHP
DNVAQSLIHG VKSGKFSFTN EPILDVLRLI ANGISPRENS AVEFLLMPFC FLFQVIYLFY
MDYVVFQSGA KATKSKSQ
//
