SDSL_HUMAN
ID SDSL_HUMAN Reviewed; 329 AA.
AC Q96GA7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine dehydratase-like;
DE AltName: Full=L-serine deaminase;
DE AltName: Full=L-serine dehydratase/L-threonine deaminase;
DE AltName: Full=L-threonine dehydratase;
DE Short=TDH;
DE EC=4.3.1.19;
DE AltName: Full=Serine dehydratase 2;
DE Short=SDH 2;
DE EC=4.3.1.17;
GN Name=SDSL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gong R.M., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Homo sapiens serine
RT dehydratase.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-328 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLY-72 AND
RP CYS-309.
RX PubMed=18342636; DOI=10.1016/j.bbagen.2008.01.020;
RA Yamada T., Komoto J., Kasuya T., Takata Y., Ogawa H., Mori H.,
RA Takusagawa F.;
RT "A catalytic mechanism that explains a low catalytic activity of serine
RT dehydratase like-1 from human cancer cells: crystal structure and site-
RT directed mutagenesis studies.";
RL Biochim. Biophys. Acta 1780:809-818(2008).
CC -!- FUNCTION: Has low serine dehydratase and threonine dehydratase
CC activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC Evidence={ECO:0000269|PubMed:18342636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC Evidence={ECO:0000269|PubMed:18342636};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 mM for serine;
CC KM=7 mM for threonine;
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:18342636}.
CC -!- INTERACTION:
CC Q96GA7; Q96GA7: SDSL; NbExp=6; IntAct=EBI-744440, EBI-744440;
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; AF134473; AAP97250.1; -; mRNA.
DR EMBL; BC009849; AAH09849.1; -; mRNA.
DR EMBL; BC091479; AAH91479.1; -; mRNA.
DR CCDS; CCDS9170.1; -.
DR RefSeq; NP_001291922.1; NM_001304993.1.
DR RefSeq; NP_612441.1; NM_138432.3.
DR RefSeq; XP_005253888.1; XM_005253831.4.
DR RefSeq; XP_011536148.1; XM_011537846.2.
DR PDB; 2RKB; X-ray; 2.80 A; A/B/C/D/E=11-328.
DR PDBsum; 2RKB; -.
DR AlphaFoldDB; Q96GA7; -.
DR SMR; Q96GA7; -.
DR BioGRID; 125255; 7.
DR IntAct; Q96GA7; 2.
DR STRING; 9606.ENSP00000385790; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR iPTMnet; Q96GA7; -.
DR MetOSite; Q96GA7; -.
DR PhosphoSitePlus; Q96GA7; -.
DR BioMuta; SDSL; -.
DR DMDM; 74731799; -.
DR EPD; Q96GA7; -.
DR jPOST; Q96GA7; -.
DR MassIVE; Q96GA7; -.
DR MaxQB; Q96GA7; -.
DR PaxDb; Q96GA7; -.
DR PeptideAtlas; Q96GA7; -.
DR PRIDE; Q96GA7; -.
DR ProteomicsDB; 76609; -.
DR Antibodypedia; 31274; 300 antibodies from 26 providers.
DR DNASU; 113675; -.
DR Ensembl; ENST00000345635.8; ENSP00000341117.4; ENSG00000139410.15.
DR Ensembl; ENST00000403593.9; ENSP00000385790.4; ENSG00000139410.15.
DR GeneID; 113675; -.
DR KEGG; hsa:113675; -.
DR MANE-Select; ENST00000403593.9; ENSP00000385790.4; NM_001304993.2; NP_001291922.1.
DR UCSC; uc009zwh.4; human.
DR CTD; 113675; -.
DR DisGeNET; 113675; -.
DR GeneCards; SDSL; -.
DR HGNC; HGNC:30404; SDSL.
DR HPA; ENSG00000139410; Tissue enhanced (liver).
DR neXtProt; NX_Q96GA7; -.
DR OpenTargets; ENSG00000139410; -.
DR PharmGKB; PA134862016; -.
DR VEuPathDB; HostDB:ENSG00000139410; -.
DR eggNOG; KOG1250; Eukaryota.
DR GeneTree; ENSGT00940000160713; -.
DR HOGENOM; CLU_021152_3_0_1; -.
DR InParanoid; Q96GA7; -.
DR OMA; DALQPCG; -.
DR OrthoDB; 1199679at2759; -.
DR PhylomeDB; Q96GA7; -.
DR TreeFam; TF329014; -.
DR BioCyc; MetaCyc:HS06616-MON; -.
DR BRENDA; 4.3.1.17; 2681.
DR PathwayCommons; Q96GA7; -.
DR Reactome; R-HSA-8849175; Threonine catabolism.
DR SABIO-RK; Q96GA7; -.
DR SignaLink; Q96GA7; -.
DR BioGRID-ORCS; 113675; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; SDSL; human.
DR EvolutionaryTrace; Q96GA7; -.
DR GenomeRNAi; 113675; -.
DR Pharos; Q96GA7; Tbio.
DR PRO; PR:Q96GA7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96GA7; protein.
DR Bgee; ENSG00000139410; Expressed in right lobe of liver and 106 other tissues.
DR ExpressionAtlas; Q96GA7; baseline and differential.
DR Genevisible; Q96GA7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Lipid metabolism; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..329
FT /note="Serine dehydratase-like"
FT /id="PRO_0000264624"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 72
FT /note="G->A: Strongly increased enzyme activity towards
FT threonine."
FT /evidence="ECO:0000269|PubMed:18342636"
FT MUTAGEN 309
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:18342636"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 254..268
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:2RKB"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2RKB"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:2RKB"
SQ SEQUENCE 329 AA; 34674 MW; CEAD30E570A43B7E CRC64;
MDGPVAEHAK QEPFHVVTPL LESWALSQVA GMPVFLKCEN VQPSGSFKIR GIGHFCQEMA
KKGCRHLVCS SGGNAGIAAA YAARKLGIPA TIVLPESTSL QVVQRLQGEG AEVQLTGKVW
DEANLRAQEL AKRDGWENVP PFDHPLIWKG HASLVQELKA VLRTPPGALV LAVGGGGLLA
GVVAGLLEVG WQHVPIIAME THGAHCFNAA ITAGKLVTLP DITSVAKSLG AKTVAARALE
CMQVCKIHSE VVEDTEAVSA VQQLLDDERM LVEPACGAAL AAIYSGLLRR LQAEGCLPPS
LTSVVVIVCG GNNINSRELQ ALKTHLGQV
