ID A0A1F5LTI2_9EURO Unreviewed; 489 AA.
AC A0A1F5LTI2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN ORFNames=PENARI_c003G11776 {ECO:0000313|EMBL:OGE56406.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE56406.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE56406.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE56406.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:76941, ChEBI:CHEBI:84410, ChEBI:CHEBI:456216;
CC EC=2.7.1.91; Evidence={ECO:0000256|ARBA:ARBA00043822};
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:OGE56406.1}.
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DR EMBL; LXJU01000003; OGE56406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LTI2; -.
DR STRING; 1835702.A0A1F5LTI2; -.
DR OrthoDB; 374620at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF31; LD11247P-RELATED; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 118..257
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 489 AA; 52995 MW; 248E56A520D0F64B CRC64;
MSTADTAQDA HDSTVTVDSV SLTLGTDSLL IVDDRSARPN RHCCGLFKSA PQTTHAISLY
NVLGAEVTAS NLVIAYAQPA GKDDVAVATV QYPVVEKEKK LVEAWVGKLI DSAYGKAIRG
KRLKVLVNPF GGKGTAASLY QRYAAPVFAA AKCQVDVQST EHRGHAIDIA EKLDVDAYDA
IVCCSGDGLP YEVFNGLGKR PDARTALVKT AIALLPCGSG NGMTWNAFGT GSVSIAALAI
VKGLRTPLDL VSISQKNSRT LSFLSQSFGI VAESDLATEN IRWMGAQRFT YGFLVRLMRQ
TIWPCDLAVK VEIGDKEAIK EHYATWSTRP EESDVDIKRL EAAAQSPELP ELKYGSVTDD
VPSDWQVVPG ETMGNFYAGN MAIMSKDTNM FPATLPDDGL MDVVTIDGRV SRGTAITMMN
EIPSGRFFDM PELNIRKASA YRLVPHQKEG YISIDGERVP FEAFQAEVHQ GLGTILTKSD
RIYEAEGPR
//
