ID   TDCG_ECOLI              Reviewed;         454 AA.
AC   P42630; P42629; Q2M996; Q6BF45;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 4.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=L-serine dehydratase TdcG;
DE            Short=SDH;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
GN   Name=tdcG; Synonyms=yhaP, yhaQ; OrderedLocusNames=b4471, JW5520;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
RP   SEQUENCE REVISION.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
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   CHARACTERIZATION.
RX   PubMed=9484901; DOI=10.1046/j.1365-2958.1998.00696.x;
RA   Hesslinger C., Fairhurst S.A., Sawers G.;
RT   "Novel keto acid formate-lyase and propionate kinase enzymes are components
RT   of an anaerobic pathway in Escherichia coli that degrades L-threonine to
RT   propionate.";
RL   Mol. Microbiol. 27:477-492(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine = pyruvate + NH4(+); 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: Amino-acid degradation; L-threonine degradation via propanoate
CC       pathway.
CC   -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57915.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA57916.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA57916.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U18997; AAA57915.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAT48169.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77160.1; -; Genomic_DNA.
DR   RefSeq; WP_000622126.1; NZ_CP009789.1.
DR   RefSeq; YP_026204.1; NC_000913.3.
DR   AlphaFoldDB; P42630; -.
DR   SMR; P42630; -.
DR   BioGRID; 4259263; 10.
DR   BioGRID; 853471; 2.
DR   DIP; DIP-10974N; -.
DR   FunCoup; P42630; 298.
DR   IntAct; P42630; 3.
DR   STRING; 511145.b4471; -.
DR   jPOST; P42630; -.
DR   PaxDb; 511145-b4471; -.
DR   EnsemblBacteria; AAT48169; AAT48169; b4471.
DR   GeneID; 2847724; -.
DR   KEGG; ecj:JW5520; -.
DR   KEGG; eco:b4471; -.
DR   KEGG; ecoc:C3026_16975; -.
DR   PATRIC; fig|511145.12.peg.3206; -.
DR   EchoBASE; EB2610; -.
DR   eggNOG; COG1760; Bacteria.
DR   HOGENOM; CLU_022305_0_1_6; -.
DR   InParanoid; P42630; -.
DR   OMA; WAAMREC; -.
DR   OrthoDB; 9805537at2; -.
DR   PhylomeDB; P42630; -.
DR   BioCyc; EcoCyc:LSERINEDEAM3-MONOMER; -.
DR   BioCyc; MetaCyc:LSERINEDEAM3-MONOMER; -.
DR   BRENDA; 4.3.1.17; 2026.
DR   UniPathway; UPA00052; -.
DR   PRO; PR:P42630; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P42630; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:EcoCyc.
DR   GO; GO:0009063; P:amino acid catabolic process; IDA:EcoCyc.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   FunFam; 3.30.1330.90:FF:000001; L-serine ammonia-lyase 1; 1.
DR   Gene3D; 3.30.1330.90; D-3-phosphoglycerate dehydrogenase, domain 3; 1.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR051318; Fe-S_L-Ser.
DR   InterPro; IPR004644; Fe-S_L-Ser_mono.
DR   InterPro; IPR005130; Ser_deHydtase-like_asu.
DR   InterPro; IPR005131; Ser_deHydtase_bsu.
DR   NCBIfam; NF011614; PRK15040.1; 1.
DR   NCBIfam; TIGR00720; sda_mono; 1.
DR   PANTHER; PTHR30182; L-SERINE DEHYDRATASE; 1.
DR   PANTHER; PTHR30182:SF6; L-SERINE DEHYDRATASE TDCG; 1.
DR   Pfam; PF03313; SDH_alpha; 1.
DR   Pfam; PF03315; SDH_beta; 1.
DR   SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Gluconeogenesis; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..454
FT                   /note="L-serine dehydratase TdcG"
FT                   /id="PRO_0000171905"
SQ   SEQUENCE   454 AA;  48522 MW;  AB44206A490456F4 CRC64;
     MISAFDIFKI GIGPSSSHTV GPMNAGKSFI DRLESSGLLT ATSHIVVDLY GSLSLTGKGH
     ATDVAIIMGL AGNSPQDVVI DEIPAFIELV TRSGRLPVAS GAHIVDFPVA KNIIFHPEML
     PRHENGMRIT AWKGQEELLS KTYYSVGGGF IVEEEHFGLS HDVETSVPYD FHSAGELLKM
     CDYNGLSISG LMMHNELALR SKAEIDAGFA RIWQVMHDGI ERGMNTEGVL PGPLNVPRRA
     VALRRQLVSS DNISNDPMNV IDWINMYALA VSEENAAGGR VVTAPTNGAC GIIPAVLAYY
     DKFRRPVNER SIARYFLAAG AIGALYKMNA SISGAEVGCQ GEIGVACSMA AAGLTELLGG
     SPAQVCNAAE IAMEHNLGLT CDPVAGQVQI PCIERNAINA VKAVNAARMA MRRTSAPRVS
     LDKVIETMYE TGKDMNDKYR ETSRGGLAIK VVCG
//