SPT_CAUVN
ID SPT_CAUVN Reviewed; 404 AA.
AC A0A0H3C7E9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Serine palmitoyltransferase {ECO:0000303|PubMed:33063925, ECO:0000303|PubMed:34969973};
DE EC=2.3.1.50 {ECO:0000269|PubMed:34969973};
GN Name=spt {ECO:0000303|PubMed:33063925, ECO:0000303|PubMed:34969973};
GN OrderedLocusNames=CCNA_01220 {ECO:0000312|EMBL:ACL94685.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=33063925; DOI=10.1111/1462-2920.15280;
RA Olea-Ozuna R.J., Poggio S., Bergstroem E., Quiroz-Rocha E.,
RA Garcia-Soriano D.A., Sahonero-Canavesi D.X., Padilla-Gomez J.,
RA Martinez-Aguilar L., Lopez-Lara I.M., Thomas-Oates J., Geiger O.;
RT "Five structural genes required for ceramide synthesis in Caulobacter and
RT for bacterial survival.";
RL Environ. Microbiol. 23:143-159(2021).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=NA1000 / CB15N;
RX PubMed=34969973; DOI=10.1038/s41589-021-00948-7;
RA Stankeviciute G., Tang P., Ashley B., Chamberlain J.D., Hansen M.E.B.,
RA Coleman A., D'Emilia R., Fu L., Mohan E.C., Nguyen H., Guan Z.,
RA Campopiano D.J., Klein E.A.;
RT "Convergent evolution of bacterial ceramide synthesis.";
RL Nat. Chem. Biol. 18:305-312(2022).
CC -!- FUNCTION: Involved in de novo bacterial ceramide synthesis
CC (PubMed:33063925, PubMed:34969973). Catalyzes the condensation of L-
CC serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-
CC oxosphinganine (PubMed:34969973). Can also condense serine and C16:1-
CC CoA, but shows a preference for palmitoyl-CoA (PubMed:34969973).
CC {ECO:0000269|PubMed:33063925, ECO:0000269|PubMed:34969973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299; EC=2.3.1.50;
CC Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P12998};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for hexadecanoyl-CoA {ECO:0000269|PubMed:34969973};
CC KM=2.98 mM for L-serine {ECO:0000269|PubMed:34969973};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:34969973}.
CC -!- DISRUPTION PHENOTYPE: Survival of the spt-deficient mutant is much
CC reduced, in comparison with wild type, during stationary phase of
CC growth, especially at elevated temperatures (PubMed:33063925). Mutants
CC are resistant towards the antibiotic polymyxin B (PubMed:33063925).
CC Mutation causes hypersensitivity to antibiotics which affect disparate
CC processes in different cellular compartments (PubMed:33063925).
CC {ECO:0000269|PubMed:33063925}.
CC -!- MISCELLANEOUS: The bacterial ceramide synthesis pathway operates in a
CC different order from that in eukaryotes. Furthermore, phylogenetic
CC analyses support the hypothesis that the bacterial and eukaryotic
CC ceramide pathways evolved independently. {ECO:0000269|PubMed:34969973}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001340; ACL94685.1; -; Genomic_DNA.
DR RefSeq; WP_010919046.1; NC_011916.1.
DR RefSeq; YP_002516593.1; NC_011916.1.
DR SMR; A0A0H3C7E9; -.
DR EnsemblBacteria; ACL94685; ACL94685; CCNA_01220.
DR GeneID; 7333613; -.
DR KEGG; ccs:CCNA_01220; -.
DR PATRIC; fig|565050.3.peg.1202; -.
DR HOGENOM; CLU_015846_11_0_5; -.
DR OMA; RSQMFAK; -.
DR OrthoDB; 479874at2; -.
DR PhylomeDB; A0A0H3C7E9; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Lipid metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Serine palmitoyltransferase"
FT /id="PRO_0000455452"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 185
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 213
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12998"
SQ SEQUENCE 404 AA; 43460 MW; 32073CE7FF55B2CD CRC64;
MGLFDKHLAY RDAYKAIQDV GANPFKVRFD AVHSPTEGVV DGRPTILLGT NNYLGLTFDE
QAIAASVKAV QERGTGTTGS RIANGSFESH VELEQELAKF YGRKHAMVFT TGYQANLGVL
STLVGRGDHL ILDADSHASI YDGSRLGHAE VIRFRHNDPE DLAKRLRRLG DAPGERLIVV
EGIYSMIGDV APLKEIAAVK REMGGYLLVD EAHSMGVLGA TGRGLAEAAG VEEDVDFIVG
TFSKSLGAIG GFCVSDHDDF DVMRVICRPY MFTASLPPAV AASTVTALRR MIEQPELRDR
LNRNAKRLYD GLTAMGFLTG PSASPIVAAT MPDQERAIAM WNGLLQAGVY LNLALPPATP
DSRPLLRASV SAAHTDEQID AVLKTYGEIG AALGVIEPLK RARA
