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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei203 – 2031Schiff-base intermediate with substrateBy similarity
Binding sitei213 – 2131Substrate 1By similarity
Binding sitei224 – 2241Substrate 1By similarity
Metal bindingi240 – 2401MagnesiumBy similarity
Active sitei255 – 2551Schiff-base intermediate with substrateBy similarity
Binding sitei281 – 2811Substrate 2By similarity
Binding sitei320 – 3201Substrate 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. porphobilinogen synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:hemB
Ordered Locus Names:SCO3311
ORF Names:SCE68.09c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Delta-aminolevulinic acid dehydratasePRO_0000140519Add
BLAST

Proteomic databases

PRIDEiP54919.

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi100226.SCO3311.

Structurei

3D structure databases

ProteinModelPortaliP54919.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiP54919.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.
PhylomeDBiP54919.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTYGSFPGA RPRRLRTTPV MRRMVAETRL HPADFILPAF VREGVSEPVP
60 70 80 90 100
IAAMPGVVQH TRDTLKKAAA EAVEAGVSGI MLFGVPEDGK KDAAGTAGTD
110 120 130 140 150
PDGILQVALR DVRAEVGDEL LVMSDLCLDE FTDHGHCGVL DGQGRVDNDA
160 170 180 190 200
TLERYAEMAQ VQADAGAHVV GPSGMMDGQI GVIRDALDQI GREDVAILAY
210 220 230 240 250
TAKYASAFYG PFREAVGSSL KGDRKTYQQD SANARESLRE LALDLEEGAD
260 270 280 290 300
MVMVKPAGPY LDILAKVAEA SDVPVAAYQI SGEYSMIEAA AEKGWIDRDR
310 320 330
AILESLTGIK RAGARNILTY WATEVARTLR
Length:330
Mass (Da):35,453
Last modified:December 1, 2000 - v2
Checksum:iD2AF1F8B971F30F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001D → V in AAA61398 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19249 Genomic DNA. Translation: AAA61398.1.
AL939116 Genomic DNA. Translation: CAB45345.1.
PIRiT36259.
RefSeqiNP_627521.1. NC_003888.3.

Genome annotation databases

GeneIDi1098745.
KEGGisco:SCO3311.
PATRICi23736366. VBIStrCoe124346_3371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19249 Genomic DNA. Translation: AAA61398.1.
AL939116 Genomic DNA. Translation: CAB45345.1.
PIRiT36259.
RefSeqiNP_627521.1. NC_003888.3.

3D structure databases

ProteinModelPortaliP54919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO3311.

Proteomic databases

PRIDEiP54919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1098745.
KEGGisco:SCO3311.
PATRICi23736366. VBIStrCoe124346_3371.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiP54919.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.
PhylomeDBiP54919.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterisation of the genes that encode enzymes for first steps of tetrapyrrole biosynthesis in Streptomyces coelicolor A3(2)."
    Petricek M.
    Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A3(2) / NRRL B-16638.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiHEM2_STRCO
AccessioniPrimary (citable) accession number: P54919
Secondary accession number(s): Q9S2E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: April 29, 2015
This is version 96 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.