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Protein

L-serine dehydratase 2

Gene

sdaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Deaminates also threonine, particularly when it is present in high concentration.

Catalytic activityi

L-serine = pyruvate + NH3.

Cofactori

[4Fe-4S] clusterCuratedNote: Binds 1 [4Fe-4S] cluster.Curated

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • L-serine ammonia-lyase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • gluconeogenesis Source: UniProtKB-UniPathway
  • L-serine catabolic process Source: EcoCyc

Keywordsi

Molecular functionLyase
Biological processGluconeogenesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:LSERINEDEAM2-MONOMER
MetaCyc:LSERINEDEAM2-MONOMER
BRENDAi4.3.1.17 2026
UniPathwayiUPA00138

Names & Taxonomyi

Protein namesi
Recommended name:
L-serine dehydratase 2 (EC:4.3.1.17)
Short name:
SDH 2
Alternative name(s):
L-serine deaminase 2
Short name:
L-SD2
Gene namesi
Name:sdaB
Ordered Locus Names:b2797, JW2768
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11623 sdaB

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001719041 – 455L-serine dehydratase 2Add BLAST455

Post-translational modificationi

Activated by post-translational modification by a system involving at least three gene products. Activation is mimicked in vitro by iron and dithiothreitol. There is considerable evidence for a free-radical activation mechanism.

Proteomic databases

PaxDbiP30744
PRIDEiP30744

Expressioni

Inductioni

Transcribed in rich medium, particularly in the absence of glucose, and is under the control of catabolite activator protein. It is made aerobically and anaerobically. Repressed by LeuO. Part of the sdaCB operon.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4261306, 9 interactors
IntActiP30744, 2 interactors
STRINGi316385.ECDH10B_2966

Structurei

3D structure databases

ProteinModelPortaliP30744
SMRiP30744
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EJQ Bacteria
COG1760 LUCA
HOGENOMiHOG000036732
InParanoidiP30744
KOiK01752
OMAiELHRDTY
PhylomeDBiP30744

Family and domain databases

Gene3Di3.30.1330.90, 1 hit
InterProiView protein in InterPro
IPR029009 ASB_dom_sf
IPR004644 Fe-S_L-Ser_mono
IPR005130 Ser_deHydtase-like_asu
IPR005131 Ser_deHydtase_bsu
PfamiView protein in Pfam
PF03313 SDH_alpha, 1 hit
PF03315 SDH_beta, 1 hit
SUPFAMiSSF143548 SSF143548, 1 hit
TIGRFAMsiTIGR00720 sda_mono, 1 hit

Sequencei

Sequence statusi: Complete.

P30744-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISVFDIFKI GIGPSSSHTV GPMKAGKQFT DDLIARNLLK DVTRVVVDVY
60 70 80 90 100
GSLSLTGKGH HTDIAIIMGL AGNLPDTVDI DSIPSFIQDV NTHGRLMLAN
110 120 130 140 150
GQHEVEFPVD QCMNFHADNL SLHENGMRIT ALAGDKVVYS QTYYSIGGGF
160 170 180 190 200
IVDEEHFGQQ DSAPVEVPYP YSSAADLQKH CQETGLSLSG LMMKNELALH
210 220 230 240 250
SKEELEQHLA NVWEVMRGGI ERGISTEGVL PGKLRVPRRA AALRRMLVSQ
260 270 280 290 300
DKTTTDPMAV VDWINMFALA VNEENAAGGR VVTAPTNGAC GIIPAVLAYY
310 320 330 340 350
DKFIREVNAN SLARYLLVAS AIGSLYKMNA SISGAEVGCQ GEVGVACSMA
360 370 380 390 400
AAGLAELLGA SPAQVCIAAE IAMEHNLGLT CDPVAGQVQV PCIERNAIAA
410 420 430 440 450
VKAVNAARMA LRRTSEPRVC LDKVIETMYE TGKDMNAKYR ETSRGGLAMK

IVACD
Length:455
Mass (Da):48,753
Last modified:November 1, 1997 - v2
Checksum:i47BCD8E880202008
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132L → V (PubMed:8385012).Curated1
Sequence conflicti134G → A (PubMed:8385012).Curated1
Sequence conflicti196 – 197EL → DV (PubMed:8385012).Curated2
Sequence conflicti236 – 239VPRR → STPC (PubMed:8385012).Curated4
Sequence conflicti360 – 362ASP → GNR (PubMed:8385012).Curated3
Sequence conflicti372A → G (PubMed:8385012).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07763 Genomic DNA No translation available.
U29581 Genomic DNA Translation: AAB40447.1
U00096 Genomic DNA Translation: AAC75839.1
AP009048 Genomic DNA Translation: BAE76869.1
PIRiA65062
RefSeqiNP_417277.1, NC_000913.3
WP_000626422.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75839; AAC75839; b2797
BAE76869; BAE76869; BAE76869
GeneIDi947262
KEGGiecj:JW2768
eco:b2797
PATRICifig|1411691.4.peg.3936

Similar proteinsi

Entry informationi

Entry nameiSDHM_ECOLI
AccessioniPrimary (citable) accession number: P30744
Secondary accession number(s): Q2MA37, Q59377
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 133 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health