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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Chlamydia muridarum (strain MoPn / Nigg)
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 sitei199 – 1991Schiff-base intermediate with substrateBy similarity
Binding sitei209 – 2091Substrate 1By similarity
Binding sitei221 – 2211Substrate 1By similarity
Metal bindingi237 – 2371MagnesiumBy similarity
Active sitei252 – 2521Schiff-base intermediate with substrateBy similarity
Binding sitei278 – 2781Substrate 2By similarity
Binding sitei317 – 3171Substrate 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

BioCyciCMUR243161:GHYU-1-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:TC_0001
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000800 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Delta-aminolevulinic acid dehydratasePRO_0000140495Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi243161.TC0001.

Structurei

3D structure databases

ProteinModelPortaliQ9PLU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.

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.

Q9PLU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLPLLKRP RRNRKSAAIR SMIRETNMVS SDLIWPIFLK EGSGIREEIP
60 70 80 90 100
SMPGVYRWSL DTISRELERL CLIGLKAVIL FPVIEDQKKD QFGAYASHPY
110 120 130 140 150
NIVCRGIQEI KKSFPQLCVI SDIALDPFTT SGHDGIFYNN EVLNDESVRV
160 170 180 190 200
YGDIATLHAE MGADIVAPSD MMDGRVRHIR EKMDQMGFVN TGILSYSAKY
210 220 230 240 250
ASYLYGPFRD ALSSHPQSGD KRQYQMDPAN VREALLECRL DEEEGADMVM
260 270 280 290 300
IKPAGFYLDV IMKAQECTHL PVVAYQVSGE YSMIMAASLH GWLSKEGAIS
310 320 330
ESLLAIKRAG ATAIISYATP WVLEWLARDA LPF
Length:333
Mass (Da):37,450
Last modified:October 1, 2000 - v1
Checksum:i905DC8BCE50B87B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF38895.1.
PIRiB81751.
RefSeqiNP_296385.1. NC_002620.2.

Genome annotation databases

EnsemblBacteriaiAAF38895; AAF38895; TC_0001.
KEGGicmu:TC_0001.
PATRICi20371336. VBIChlMur19118_0011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF38895.1.
PIRiB81751.
RefSeqiNP_296385.1. NC_002620.2.

3D structure databases

ProteinModelPortaliQ9PLU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243161.TC0001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF38895; AAF38895; TC_0001.
KEGGicmu:TC_0001.
PATRICi20371336. VBIChlMur19118_0011.

Phylogenomic databases

eggNOGiCOG0113.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciCMUR243161:GHYU-1-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MoPn / Nigg.

Entry informationi

Entry nameiHEM2_CHLMU
AccessioniPrimary (citable) accession number: Q9PLU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete 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.