TSC10_EMENI
ID TSC10_EMENI Reviewed; 369 AA.
AC Q5BE65; C8VT29;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=3-ketodihydrosphingosine reductase tsc10;
DE EC=1.1.1.102;
DE AltName: Full=3-dehydrosphinganine reductase;
DE AltName: Full=KDS reductase;
GN Name=tsc10; ORFNames=AN1165;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to
CC dihydrosphingosine (DHS). {ECO:0000250}.
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;
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA66283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000016; EAA66283.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001308; CBF88015.1; -; Genomic_DNA.
DR RefSeq; XP_658769.1; XM_653677.1.
DR AlphaFoldDB; Q5BE65; -.
DR SMR; Q5BE65; -.
DR STRING; 162425.CADANIAP00001461; -.
DR EnsemblFungi; CBF88015; CBF88015; ANIA_01165.
DR EnsemblFungi; EAA66283; EAA66283; AN1165.2.
DR GeneID; 2876943; -.
DR KEGG; ani:AN1165.2; -.
DR VEuPathDB; FungiDB:AN1165; -.
DR eggNOG; KOG1210; Eukaryota.
DR HOGENOM; CLU_010194_3_0_1; -.
DR InParanoid; Q5BE65; -.
DR OMA; NCAGMAI; -.
DR OrthoDB; 1210617at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IBA:GO_Central.
DR GO; GO:0006666; P:3-keto-sphinganine metabolic process; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR CDD; cd08939; KDSR-like_SDR_c; 1.
DR InterPro; IPR045022; KDSR-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..369
FT /note="3-ketodihydrosphingosine reductase tsc10"
FT /id="PRO_0000054796"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT /evidence="ECO:0000250"
FT BINDING 52..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 40461 MW; 2164CE34ACCD0884 CRC64;
MHPSLPSIIY DASPTALGIS AVFGALFFYT LVKMFGFLAR ENQFVVEGRT VVITGGSEGM
GKAVACQLAQ KGANIVIVAR TLQKLEEAIE AIKGSAANVN KQRFHYISAD LTKPEECERI
MTEVTEWNDG MPPDIVWCCA GYCTPGYFVE TSVQTLKDQM DTVYWTAANT AHAILRKWLV
PINPSHQRPL PRRHLIFTCS TLAFVPIAGY APYSPAKAAM RALSDTLCQE IEVYNGSRAS
KERARATPAD VKIHTVFPMG ILSPGFDNEQ QIKPALTKQL ESADKPQTPK EVARIAIEAI
ERGEYLITTM FVGDVMKGAA LGPSPRNSWF RDTCTGWLSN LLFLGVVPDL RKQAFNWGAK
NGVPTSPSA
