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Protein

L-serine dehydratase 2

Gene

sdaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:LSERINEDEAM2-MONOMER.
ECOL316407:JW2768-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11623. sdaB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455L-serine dehydratase 2PRO_0000171904Add
BLAST

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 interactions.
IntActiP30744. 2 interactions.
STRINGi511145.b2797.

Structurei

3D structure databases

ProteinModelPortaliP30744.
SMRiP30744. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EJQ. Bacteria.
COG1760. LUCA.
HOGENOMiHOG000036732.
InParanoidiP30744.
KOiK01752.
OMAiLENELTW.
PhylomeDBiP30744.

Family and domain databases

Gene3Di3.30.1330.90. 1 hit.
InterProiIPR029009. ASB_dom.
IPR004644. Fe-S_L-Ser_mono.
IPR005130. Ser_deHydtase-like_asu.
IPR005131. Ser_deHydtase_bsu.
[Graphical view]
PfamiPF03313. SDH_alpha. 1 hit.
PF03315. SDH_beta. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321L → V (PubMed:8385012).Curated
Sequence conflicti134 – 1341G → A (PubMed:8385012).Curated
Sequence conflicti196 – 1972EL → DV (PubMed:8385012).Curated
Sequence conflicti236 – 2394VPRR → STPC (PubMed:8385012).Curated
Sequence conflicti360 – 3623ASP → GNR (PubMed:8385012).Curated
Sequence conflicti372 – 3721A → G (PubMed:8385012).Curated

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.
PATRICi32121010. VBIEscCol129921_2897.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP30744.
SMRiP30744. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261306. 9 interactions.
IntActiP30744. 2 interactions.
STRINGi511145.b2797.

Proteomic databases

PaxDbiP30744.
PRIDEiP30744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75839; AAC75839; b2797.
BAE76869; BAE76869; BAE76869.
GeneIDi947262.
KEGGiecj:JW2768.
eco:b2797.
PATRICi32121010. VBIEscCol129921_2897.

Organism-specific databases

EchoBASEiEB1580.
EcoGeneiEG11623. sdaB.

Phylogenomic databases

eggNOGiENOG4105EJQ. Bacteria.
COG1760. LUCA.
HOGENOMiHOG000036732.
InParanoidiP30744.
KOiK01752.
OMAiLENELTW.
PhylomeDBiP30744.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciEcoCyc:LSERINEDEAM2-MONOMER.
ECOL316407:JW2768-MONOMER.
MetaCyc:LSERINEDEAM2-MONOMER.
BRENDAi4.3.1.17. 2026.

Miscellaneous databases

PROiP30744.

Family and domain databases

Gene3Di3.30.1330.90. 1 hit.
InterProiIPR029009. ASB_dom.
IPR004644. Fe-S_L-Ser_mono.
IPR005130. Ser_deHydtase-like_asu.
IPR005131. Ser_deHydtase_bsu.
[Graphical view]
PfamiPF03313. SDH_alpha. 1 hit.
PF03315. SDH_beta. 1 hit.
[Graphical view]
SUPFAMiSSF143548. SSF143548. 1 hit.
TIGRFAMsiTIGR00720. sda_mono. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSDHM_ECOLI
AccessioniPrimary (citable) accession number: P30744
Secondary accession number(s): Q2MA37, Q59377
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.