SDHM_ECOLI
ID SDHM_ECOLI Reviewed; 455 AA.
AC P30744; Q2MA37; Q59377;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=L-serine dehydratase 2;
DE Short=SDH 2;
DE EC=4.3.1.17;
DE AltName: Full=L-serine deaminase 2;
DE Short=L-SD2;
GN Name=sdaB; OrderedLocusNames=b2797, JW2768;
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=8385012; DOI=10.1111/j.1432-1033.1993.tb17718.x;
RA Shao Z., Newman E.B.;
RT "Sequencing and characterization of the sdaB gene from Escherichia coli K-
RT 12.";
RL Eur. J. Biochem. 212:777-784(1993).
RN [2]
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 [3]
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).
RN [4]
RP OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
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: Transcribed in rich medium, particularly in the absence of
CC glucose, and is under the control of catabolite activator protein. It
CC is made aerobically and anaerobically. Repressed by LeuO. Part of the
CC sdaCB operon. {ECO:0000269|PubMed:19429622}.
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; L07763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U29581; AAB40447.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75839.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76869.1; -; Genomic_DNA.
DR PIR; A65062; A65062.
DR RefSeq; NP_417277.1; NC_000913.3.
DR RefSeq; WP_000626422.1; NZ_LN832404.1.
DR AlphaFoldDB; P30744; -.
DR SMR; P30744; -.
DR BioGRID; 4261306; 9.
DR IntAct; P30744; 2.
DR STRING; 511145.b2797; -.
DR jPOST; P30744; -.
DR PaxDb; P30744; -.
DR PRIDE; P30744; -.
DR EnsemblBacteria; AAC75839; AAC75839; b2797.
DR EnsemblBacteria; BAE76869; BAE76869; BAE76869.
DR GeneID; 947262; -.
DR KEGG; ecj:JW2768; -.
DR KEGG; eco:b2797; -.
DR PATRIC; fig|1411691.4.peg.3936; -.
DR EchoBASE; EB1580; -.
DR eggNOG; COG1760; Bacteria.
DR HOGENOM; CLU_022305_0_1_6; -.
DR InParanoid; P30744; -.
DR OMA; ELHRDTY; -.
DR PhylomeDB; P30744; -.
DR BioCyc; EcoCyc:LSERINEDEAM2-MON; -.
DR BioCyc; MetaCyc:LSERINEDEAM2-MON; -.
DR BRENDA; 4.3.1.17; 2026.
DR UniPathway; UPA00138; -.
DR PRO; PR:P30744; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 2: Evidence at transcript level;
KW 4Fe-4S; Gluconeogenesis; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..455
FT /note="L-serine dehydratase 2"
FT /id="PRO_0000171904"
FT CONFLICT 132
FT /note="L -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="G -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 196..197
FT /note="EL -> DV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 236..239
FT /note="VPRR -> STPC (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 360..362
FT /note="ASP -> GNR (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="A -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 48753 MW; 47BCD8E880202008 CRC64;
MISVFDIFKI GIGPSSSHTV GPMKAGKQFT DDLIARNLLK DVTRVVVDVY GSLSLTGKGH
HTDIAIIMGL AGNLPDTVDI DSIPSFIQDV NTHGRLMLAN GQHEVEFPVD QCMNFHADNL
SLHENGMRIT ALAGDKVVYS QTYYSIGGGF IVDEEHFGQQ DSAPVEVPYP YSSAADLQKH
CQETGLSLSG LMMKNELALH SKEELEQHLA NVWEVMRGGI ERGISTEGVL PGKLRVPRRA
AALRRMLVSQ DKTTTDPMAV VDWINMFALA VNEENAAGGR VVTAPTNGAC GIIPAVLAYY
DKFIREVNAN SLARYLLVAS AIGSLYKMNA SISGAEVGCQ GEVGVACSMA AAGLAELLGA
SPAQVCIAAE IAMEHNLGLT CDPVAGQVQV PCIERNAIAA VKAVNAARMA LRRTSEPRVC
LDKVIETMYE TGKDMNAKYR ETSRGGLAMK IVACD
