TDCG_ECOLI
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 03-AUG-2022, entry version 151.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 = 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: 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_LN832404.1.
DR RefSeq; YP_026204.1; NC_000913.3.
DR AlphaFoldDB; P42630; -.
DR SMR; P42630; -.
DR BioGRID; 4259263; 9.
DR BioGRID; 853471; 2.
DR DIP; DIP-10974N; -.
DR IntAct; P42630; 3.
DR STRING; 511145.b4471; -.
DR jPOST; P42630; -.
DR PaxDb; P42630; -.
DR PRIDE; P42630; -.
DR EnsemblBacteria; AAT48169; AAT48169; b4471.
DR EnsemblBacteria; BAE77160; BAE77160; BAE77160.
DR GeneID; 2847724; -.
DR KEGG; ecj:JW5520; -.
DR KEGG; eco:b4471; -.
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; WPFYSAR; -.
DR PhylomeDB; P42630; -.
DR BioCyc; EcoCyc:LSERINEDEAM3-MON; -.
DR BioCyc; MetaCyc:LSERINEDEAM3-MON; -.
DR BRENDA; 4.3.1.17; 2026.
DR UniPathway; UPA00052; -.
DR PRO; PR:P42630; -.
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:0009063; P:cellular amino acid catabolic process; IDA:EcoCyc.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
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; 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
