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O84638 (HEM2_CHLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Delta-aminolevulinic acid dehydratase
Short name=ALAD
Short name=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:hemB
Ordered Locus Names:CT_633
OrganismChlamydia trachomatis (strain D/UW-3/Cx) [Reference proteome] [HAMAP]
Taxonomic identifier272561 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia ›

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Subunit structure

Homooctamer By similarity.

Sequence similarities

Belongs to the ALADH family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

porphobilinogen synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Delta-aminolevulinic acid dehydratase
PRO_0000140498

Sites

Active site1991Schiff-base intermediate with substrate By similarity
Active site2521Schiff-base intermediate with substrate By similarity
Metal binding2371Magnesium By similarity
Binding site2091Substrate 1 By similarity
Binding site2211Substrate 1 By similarity
Binding site2781Substrate 2 By similarity
Binding site3171Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O84638 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 83E928F68EAA63FB

FASTA33837,737
        10         20         30         40         50         60 
MIRLPLLKRP RRNRKSAAVR SIIQETQLCS SDLIWPIFLK DGSGIREEIK SMPGVYRWSL 

        70         80         90        100        110        120 
DMVSKELERL CTIGLKAVIL FPVIDANKKE QFGSYASHPY NIVCKGIQAI KKSFPELCVI 

       130        140        150        160        170        180 
SDIALDPFTT SGHDGIFHNN YVINDESVRV YGGIAVMHAE MGADIVAPSD MMDGRVKHIR 

       190        200        210        220        230        240 
EQMDQMGFVN TGILSYSAKY ASALYGPFRD ALSSHLQSGD KRTYQMDPAN VQEALLECQL 

       250        260        270        280        290        300 
DEEEGADMVM IKPAGFYLDV IVKARENTHL PVVAYQVSGE FSMIMAACLH GWLNKESVIK 

       310        320        330 
ESLLAIKRAG ATAIISYATP WVLEWLAKDA LPFERSVL

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001273 Genomic DNA. Translation: AAC68237.1.
PIRE71489.
RefSeqNP_220150.1. NC_000117.1.

3D structure databases

ProteinModelPortalO84638.
ModBaseSearch...

Protein-protein interaction databases

STRING272561.CT633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC68237; AAC68237; CT_633.
GeneID884414.
KEGGctr:CT633.
PATRIC20380898. VBIChlTra43535_0693.

Phylogenomic databases

eggNOGCOG0113.
KOK01698.
OMADVAIMSY.
ProtClustDBPRK09283.

Enzyme and pathway databases

UniPathwayUPA00251; UER00318.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_CHLTR
AccessionPrimary (citable) accession number: O84638
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: May 29, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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