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SPT_SPHMU
ID   SPT_SPHMU               Reviewed;         399 AA.
AC   A7BFV6; A0A653ZZB6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Serine palmitoyltransferase {ECO:0000303|PubMed:17557831};
DE            Short=SPT {ECO:0000303|PubMed:17557831};
DE            EC=2.3.1.50 {ECO:0000269|PubMed:17557831};
GN   Name=spt {ECO:0000303|PubMed:17557831};
GN   ORFNames=I6J33_20140 {ECO:0000312|EMBL:QRQ60415.1},
GN   NCTC11343_02561 {ECO:0000312|EMBL:SPZ86886.1},
GN   SPHINGO8BC_150128 {ECO:0000312|EMBL:VXC60648.1};
OS   Sphingobacterium multivorum.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=28454;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=GTC97;
RX   PubMed=17557831; DOI=10.1128/jb.00194-07;
RA   Ikushiro H., Islam M.M., Tojo H., Hayashi H.;
RT   "Molecular characterization of membrane-associated soluble serine
RT   palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio
RT   stolpii.";
RL   J. Bacteriol. 189:5749-5761(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11343;
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sphingobacterium sp. 8BC;
RA   Karimi E.;
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33613 / DSM 11691 / FDAARGOS_1203;
RA   Sproer C., Gronow S., Severitt S., Schroder I., Tallon L., Sadzewicz L.,
RA   Zhao X., Boylan J., Ott S., Bowen H., Vavikolanu K., Mehta A.,
RA   Aluvathingal J., Nadendla S., Lowell S., Myers T., Yan Y., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0007744|PDB:3A2B}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-399 IN COMPLEX WITH PLP-BOUND
RP   SERINE, AND SUBUNIT.
RC   STRAIN=GTC97;
RX   PubMed=19564159; DOI=10.1093/jb/mvp100;
RA   Ikushiro H., Islam M.M., Okamoto A., Hoseki J., Murakawa T., Fujii S.,
RA   Miyahara I., Hayashi H.;
RT   "Structural insights into the enzymatic mechanism of serine
RT   palmitoyltransferase from Sphingobacterium multivorum.";
RL   J. Biochem. 146:549-562(2009).
CC   -!- FUNCTION: Catalyzes the condensation of L-serine with palmitoyl-CoA
CC       (hexadecanoyl-CoA) to produce 3-oxosphinganine (PubMed:17557831).
CC       Exhibits a broad substrate specificity concerning the chain length and
CC       the degree of unsaturation of acyl-CoA (PubMed:17557831).
CC       {ECO:0000269|PubMed:17557831}.
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:17557831};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC         Evidence={ECO:0000269|PubMed:17557831};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:17557831};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.8 mM for L-serine {ECO:0000269|PubMed:17557831};
CC         KM=0.10 mM for palmitoyl-CoA {ECO:0000269|PubMed:17557831};
CC         Note=kcat is 0.12 sec(-1). {ECO:0000269|PubMed:17557831};
CC       pH dependence:
CC         Optimum pH is 7.4 to 8.0. {ECO:0000269|PubMed:17557831};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000305|PubMed:17557831}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17557831,
CC       ECO:0000269|PubMed:19564159}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17557831}. Cell
CC       inner membrane {ECO:0000269|PubMed:17557831}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:17557831}. Note=Distributed mainly near the
CC       inner membrane of the cell. {ECO:0000269|PubMed:17557831}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AB259214; BAF73751.1; -; Genomic_DNA.
DR   EMBL; UAUU01000009; SPZ86886.1; -; Genomic_DNA.
DR   EMBL; CABWMV010000007; VXC60648.1; -; Genomic_DNA.
DR   EMBL; CP069793; QRQ60415.1; -; Genomic_DNA.
DR   RefSeq; WP_046672730.1; NZ_UGYX01000002.1.
DR   PDB; 3A2B; X-ray; 2.30 A; A=2-399.
DR   PDBsum; 3A2B; -.
DR   SMR; A7BFV6; -.
DR   EnsemblBacteria; SPZ86886; SPZ86886; NCTC11343_02561.
DR   EnsemblBacteria; SUJ02286; SUJ02286; NCTC11034_01090.
DR   GeneID; 66689277; -.
DR   BRENDA; 2.3.1.50; 2288.
DR   UniPathway; UPA00222; -.
DR   EvolutionaryTrace; A7BFV6; -.
DR   PRO; PR:A7BFV6; -.
DR   Proteomes; UP000251241; Unassembled WGS sequence.
DR   GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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   3D-structure; Acyltransferase; Cell inner membrane; Cell membrane;
KW   Cytoplasm; Lipid metabolism; Membrane; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..399
FT                   /note="Serine palmitoyltransferase"
FT                   /id="PRO_0000456078"
FT   BINDING         113..114
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000305|PubMed:19564159"
FT   BINDING         213
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000305|PubMed:19564159"
FT   BINDING         241
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
FT   BINDING         243
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000305|PubMed:19564159"
FT   MOD_RES         244
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93UV0"
SQ   SEQUENCE   399 AA;  43772 MW;  E765F69D9663811E CRC64;
     MSKGKLGEKI SQFKIVEELK AKGLYAYFRP IQSKQDTEVK IDGRRVLMFG SNSYLGLTTD
     TRIIKAAQDA LEKYGTGCAG SRFLNGTLDI HVELEEKLSA YVGKEAAILF STGFQSNLGP
     LSCLMGRNDY ILLDERDHAS IIDGSRLSFS KVIKYGHNNM EDLRAKLSRL PEDSAKLICT
     DGIFSMEGDI VNLPELTSIA NEFDAAVMVD DAHSLGVIGH KGAGTASHFG LNDDVDLIMG
     TFSKSLASLG GFVAGDADVI DFLKHNARSV MFSASMTPAS VASTLKALEI IQNEPEHIEK
     LWKNTDYAKA QLLDHGFDLG ATESPILPIF IRSNEKTFWV TKMLQDDGVF VNPVVSPAVP
     AEESLIRFSL MATHTYDQID EAIEKMVKVF KQAEVETLI
 
 
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