Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191Zinc; catalyticBy similarity
Metal bindingi121 – 1211Zinc; catalyticBy similarity
Metal bindingi129 – 1291Zinc; catalyticBy similarity
Active sitei198 – 1981Schiff-base intermediate with substrateBy similarity
Binding sitei208 – 2081Substrate 1By similarity
Binding sitei220 – 2201Substrate 1By similarity
Metal bindingi236 – 2361MagnesiumBy similarity
Active sitei251 – 2511Schiff-base intermediate with substrateBy similarity
Binding sitei277 – 2771Substrate 2By similarity
Binding sitei316 – 3161Substrate 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, Zinc

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1792-MONOMER.
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:Synpcc7942_1792
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002717: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Delta-aminolevulinic acid dehydratasePRO_0000140520Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1792.

Structurei

3D structure databases

ProteinModelPortaliP43087.
SMRiP43087. Positions 5-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OrthoDBiEOG6VXFCB.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[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.

P43087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPTHRPRRL RSSETLRRMV RETTLTSADF IYPLFAVPGE GVAKEVTSMP
60 70 80 90 100
GVYQLSIDKI VEEAKEVYDL GIPSIILFGI PTDKDNDATG AWHDCGIVQK
110 120 130 140 150
AATAVKEAVP ELIVAADTCL CEYTPHGHCG YLEVGDLSGR VLNDPTLELL
160 170 180 190 200
RKTAVSQAKA GADIIAPSGM MDGFVATIRD ALDEAGFSDT PIMAYSAKYA
210 220 230 240 250
SAYYGPFRDA AESTPQFGDR RTYQMDPGNS REALKEVELD VAEGADIVMV
260 270 280 290 300
KPALSYMDII CRIKETTDLP VAAYNVSGEY SMVKAAALNG WIDEERVVLE
310 320
TLTSFKRAGA DLILTYHAKD AARWLA
Length:326
Mass (Da):35,574
Last modified:April 18, 2006 - v2
Checksum:i0C4F44658CEB37BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871A → R in CAA49892 (PubMed:8123787).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70434 Genomic DNA. Translation: CAA49892.1.
CP000100 Genomic DNA. Translation: ABB57822.1.
RefSeqiYP_400809.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB57822; ABB57822; Synpcc7942_1792.
GeneIDi3774367.
KEGGisyf:Synpcc7942_1792.
PATRICi23789009. VBISynElo51371_2028.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70434 Genomic DNA. Translation: CAA49892.1.
CP000100 Genomic DNA. Translation: ABB57822.1.
RefSeqiYP_400809.1. NC_007604.1.

3D structure databases

ProteinModelPortaliP43087.
SMRiP43087. Positions 5-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB57822; ABB57822; Synpcc7942_1792.
GeneIDi3774367.
KEGGisyf:Synpcc7942_1792.
PATRICi23789009. VBISynElo51371_2028.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OrthoDBiEOG6VXFCB.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciSYNEL:SYNPCC7942_1792-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[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 genes for tetrapyrrole biosynthesis from the cyanobacterium Anacystis nidulans R2."
    Jones M.C., Jenkins J.M., Smith A.G., Howe C.J.
    Plant Mol. Biol. 24:435-448(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.

Entry informationi

Entry nameiHEM2_SYNE7
AccessioniPrimary (citable) accession number: P43087
Secondary accession number(s): Q31M97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 18, 2006
Last modified: January 7, 2015
This is version 84 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.