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Reviewed, UniProtKB/Swiss-Prot Q9PLU4 (HEM2_CHLMU)

Last modified November 3, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Delta-aminolevulinic acid dehydratase
      Short name=ALADH
      Short name=ALAD
    EC=4.2.1.24
Alternative name(s):
    Porphobilinogen synthase
Gene names
Name: hemB
Ordered Locus Names: TC_0001
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Pathway

Porphyrin 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 processPorphyrin biosynthesis
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processporphyrin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

porphobilinogen synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Delta-aminolevulinic acid dehydratase
PRO_0000140495

Sites

Active site2521 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PLU4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 905DC8BCE50B87B5

FASTA33337,450
        10         20         30         40         50         60 
MTRLPLLKRP RRNRKSAAIR SMIRETNMVS SDLIWPIFLK EGSGIREEIP SMPGVYRWSL 

        70         80         90        100        110        120 
DTISRELERL CLIGLKAVIL FPVIEDQKKD QFGAYASHPY NIVCRGIQEI KKSFPQLCVI 

       130        140        150        160        170        180 
SDIALDPFTT SGHDGIFYNN EVLNDESVRV YGDIATLHAE MGADIVAPSD MMDGRVRHIR 

       190        200        210        220        230        240 
EKMDQMGFVN TGILSYSAKY ASYLYGPFRD ALSSHPQSGD KRQYQMDPAN VREALLECRL 

       250        260        270        280        290        300 
DEEEGADMVM IKPAGFYLDV IMKAQECTHL PVVAYQVSGE YSMIMAASLH GWLSKEGAIS 

       310        320        330 
ESLLAIKRAG ATAIISYATP WVLEWLARDA LPF 

« Hide

Cross-references

Sequence databases

AE002160 Genomic DNA. Translation: AAF38895.1.
PIRB81751.
RefSeqNP_296385.1.

3D structure databases

HSSPHSSP built from PDB template 1B4K based on UniProtKB Q59643.
ModBaseSearch...

Genome annotation databases

GeneID1245524.
GenomeReviewsGene locus TC_0001 in contig AE002160_GR.
KEGGcmu:TC0001.
TIGRTC_0001.

Phylogenomic databases

HOGENOMQ9PLU4.
OMAPELGVIT.

Enzyme and pathway databases

BioCycCMUR243161:TC_0001-MON.
BRENDA4.2.1.24. 256349.

Family and domain databases

InterProIPR001731. 4pyrrol_synth_porphobiln_synth.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11458. AlaD_dehydratase. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
ProDomPD002304. AlaD_dehydratase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_CHLMU
AccessionPrimary (citable) accession number: Q9PLU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents