SDHL_ECOLI
ID SDHL_ECOLI Reviewed; 454 AA.
AC P16095;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=L-serine dehydratase 1;
DE Short=SDH 1;
DE EC=4.3.1.17;
DE AltName: Full=L-serine deaminase 1;
DE Short=L-SD1;
GN Name=sdaA; OrderedLocusNames=b1814, JW1803;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2504697; DOI=10.1128/jb.171.9.5095-5102.1989;
RA Su H., Lang B.F., Newman E.B.;
RT "L-serine degradation in Escherichia coli K-12: cloning and sequencing of
RT the sdaA gene.";
RL J. Bacteriol. 171:5095-5102(1989).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION, AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=8436113; DOI=10.1111/j.1432-1033.1993.tb17578.x;
RA Su H., Moniakis J., Newman E.B.;
RT "Use of gene fusions of the structural gene sdaA to purify L-serine
RT deaminase 1 from Escherichia coli K-12.";
RL Eur. J. Biochem. 211:521-527(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Deaminates also threonine, particularly when it is present in
CC high concentration.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- INDUCTION: It is made aerobically and anaerobically, in minimal medium.
CC -!- PTM: Activated by post-translational modification by a system involving
CC at least three gene products. Activation is mimicked in vitro by iron
CC and dithiothreitol. There is considerable evidence for a free-radical
CC activation mechanism.
CC -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC family. {ECO:0000305}.
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DR EMBL; M28695; AAA63580.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74884.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15621.1; -; Genomic_DNA.
DR PIR; F64942; DWECL.
DR RefSeq; NP_416328.1; NC_000913.3.
DR RefSeq; WP_000624298.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P16095; -.
DR SMR; P16095; -.
DR BioGRID; 4260949; 6.
DR IntAct; P16095; 3.
DR STRING; 511145.b1814; -.
DR jPOST; P16095; -.
DR PaxDb; P16095; -.
DR PRIDE; P16095; -.
DR EnsemblBacteria; AAC74884; AAC74884; b1814.
DR EnsemblBacteria; BAA15621; BAA15621; BAA15621.
DR GeneID; 66674297; -.
DR GeneID; 946331; -.
DR KEGG; ecj:JW1803; -.
DR KEGG; eco:b1814; -.
DR PATRIC; fig|511145.12.peg.1891; -.
DR EchoBASE; EB0923; -.
DR eggNOG; COG1760; Bacteria.
DR HOGENOM; CLU_022305_0_1_6; -.
DR InParanoid; P16095; -.
DR OMA; SAAMGGC; -.
DR PhylomeDB; P16095; -.
DR BioCyc; EcoCyc:LSERINEDEAM1-MON; -.
DR BioCyc; MetaCyc:LSERINEDEAM1-MON; -.
DR BRENDA; 4.3.1.17; 2026.
DR UniPathway; UPA00138; -.
DR PRO; PR:P16095; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006565; P:L-serine catabolic process; IDA:EcoCyc.
DR Gene3D; 3.30.1330.90; -; 1.
DR InterPro; IPR029009; ASB_dom_sf.
DR InterPro; IPR004644; Fe-S_L-Ser_mono.
DR InterPro; IPR005130; Ser_deHydtase-like_asu.
DR InterPro; IPR005131; Ser_deHydtase_bsu.
DR Pfam; PF03313; SDH_alpha; 1.
DR Pfam; PF03315; SDH_beta; 1.
DR SUPFAM; SSF143548; SSF143548; 1.
DR TIGRFAMs; TIGR00720; sda_mono; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Gluconeogenesis; Iron; Iron-sulfur;
KW Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..454
FT /note="L-serine dehydratase 1"
FT /id="PRO_0000171903"
SQ SEQUENCE 454 AA; 48907 MW; B2CD530423E95BE1 CRC64;
MISLFDMFKV GIGPSSSHTV GPMKAGKQFV DDLVEKGLLD SVTRVAVDVY GSLSLTGKGH
HTDIAIIMGL AGNEPATVDI DSIPGFIRDV EERERLLLAQ GRHEVDFPRD NGMRFHNGNL
PLHENGMQIH AYNGDEVVYS KTYYSIGGGF IVDEEHFGQD AANEVSVPYP FKSATELLAY
CNETGYSLSG LAMQNELALH SKKEIDEYFA HVWQTMQACI DRGMNTEGVL PGPLRVPRRA
SALRRMLVSS DKLSNDPMNV IDWVNMFALA VNEENAAGGR VVTAPTNGAC GIVPAVLAYY
DHFIESVSPD IYTRYFMAAG AIGALYKMNA SISGAEVGCQ GEVGVACSMA AAGLAELLGG
SPEQVCVAAE IGMEHNLGLT CDPVAGQVQV PCIERNAIAS VKAINAARMA LRRTSAPRVS
LDKVIETMYE TGKDMNAKYR ETSRGGLAIK VQCD
