Reviewed, UniProtKB/Swiss-Prot P42630 (TDCG_ECOLI)

Names and origin

Protein names

Recommended name:
    L-serine dehydratase tdcG
      Short name=SDH
    EC=4.3.1.17
Alternative name(s):
    L-serine deaminase

Gene names

Name:	tdcG
Synonyms:	yhaP, yhaQ
Ordered Locus Names:	b4471, JW5520

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-serine = pyruvate + NH3.
Cofactor	Binds 1 4Fe-4S cluster Probable.
Pathway	Amino-acid degradation; L-threonine degradation via propanoate pathway.
Sequence similarities	Belongs to the iron-sulfur dependent L-serine dehydratase family.
Sequence caution	The sequence AAA57915.1 differs from that shown. Reason: Frameshift at position 133. The sequence AAA57916.1 differs from that shown. Reason: Frameshift at position 133.

Ontologies

Keywords
Biological process	Gluconeogenesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW L-serine ammonia-lyase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 454	454	L-serine dehydratase tdcG		PRO_0000171905

Sequences

	Sequence		Length	Mass (Da)
	P42630-1 [UniParc]. Last modified December 7, 2004. Version 4. Checksum: AB44206A490456F4	FASTA	454	48,522
	10 20 30 40 50 60 MISAFDIFKI GIGPSSSHTV GPMNAGKSFI DRLESSGLLT ATSHIVVDLY GSLSLTGKGH 70 80 90 100 110 120 ATDVAIIMGL AGNSPQDVVI DEIPAFIELV TRSGRLPVAS GAHIVDFPVA KNIIFHPEML 130 140 150 160 170 180 PRHENGMRIT AWKGQEELLS KTYYSVGGGF IVEEEHFGLS HDVETSVPYD FHSAGELLKM 190 200 210 220 230 240 CDYNGLSISG LMMHNELALR SKAEIDAGFA RIWQVMHDGI ERGMNTEGVL PGPLNVPRRA 250 260 270 280 290 300 VALRRQLVSS DNISNDPMNV IDWINMYALA VSEENAAGGR VVTAPTNGAC GIIPAVLAYY 310 320 330 340 350 360 DKFRRPVNER SIARYFLAAG AIGALYKMNA SISGAEVGCQ GEIGVACSMA AAGLTELLGG 370 380 390 400 410 420 SPAQVCNAAE IAMEHNLGLT CDPVAGQVQI PCIERNAINA VKAVNAARMA MRRTSAPRVS 430 440 450 LDKVIETMYE TGKDMNDKYR ETSRGGLAIK VVCG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005." Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L. Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate." Hesslinger C., Fairhurst S.A., Sawers G. Mol. Microbiol. 27:477-492(1998) [PubMed: 9484901] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U18997 Genomic DNA. Translation: AAA57916.1. Frameshift. U18997 Genomic DNA. Translation: AAA57915.1. Frameshift. U00096 Genomic DNA. Translation: AAT48169.1. AP009048 Genomic DNA. Translation: BAE77160.1.
RefSeq	AP_003659.1. YP_026204.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10974N.
STRING	P42630.
Genome annotation databases
GeneID	2847724.
GenomeReviews	Gene locus JW5520 in contig AP009048_GR. Gene locus b4471 in contig U00096_GR.
KEGG	ecj:JW5520. eco:b4471.
Organism-specific databases
EchoBASE	EB2610.
EcoGene	EG12756. tdcG.
CMR	Search...
Phylogenomic databases
HOGENOM	P42630.
OMA	LANQHRI.
Enzyme and pathway databases
BioCyc	EcoCyc:LSERINEDEAM3-MON. MetaCyc:LSERINEDEAM3-MON.
Gene expression databases
Genevestigator	P42630.
Family and domain databases
InterPro	IPR004644. Fe-S_L-Ser_mono. IPR005130. Ser_deHydtase_asu. IPR005131. Ser_deHydtase_bsu. [Graphical view]
Pfam	PF03313. SDH_alpha. 1 hit. PF03315. SDH_beta. 1 hit. [Graphical view]
TIGRFAMs	TIGR00720. sda_mono. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TDCG_ECOLI

Accession

Primary (citable) accession number: P42630
Secondary accession number(s): P42629, Q2M996, Q6BF45

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 7, 2004
Last modified:	November 3, 2009
This is version 74 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)