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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
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.

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (hemB)
  2. Probable porphobilinogen deaminase (hemC)
  3. no protein annotated in this organism
  4. Uroporphyrinogen decarboxylase (hemE)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciCPNE115711:GI7B-1-MONOMER.
CPNE115713:GHEY-777-MONOMER.
CPNE138677:GH8N-768-MONOMER.
CPNE182082:GH4N-796-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:CPn_0744, CP_0001, CpB0772
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000583 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Delta-aminolevulinic acid dehydratasePRO_0000140496Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi115713.CPn0744.

Structurei

3D structure databases

ProteinModelPortaliQ9Z7G1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
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.

Q9Z7G1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLTLSRRP RRNRKTAAIR DLLAETHLSP KDLIAPFFVK YGNNIKEEIP
60 70 80 90 100
SLPGVFRWSL DLLLKEIERL CTYGLRAVML FPIIPDDLKD AYGSYSSNPK
110 120 130 140 150
NILCHSIHEI KNAFPHLCLI SDIALDPYTT HGHDGIFLNG EVLNDESVRI
160 170 180 190 200
FGNIATLHAE MGADIVAPSD MMDGRIGYIR SKLDQSGYSK TSIMSYSVKY
210 220 230 240 250
ASCLYSPFRD ALSSHVTSGD KKQYQMNPKN VLEALLESSL DEEEGADILM
260 270 280 290 300
VKPAGLYLDV IYRIRQNTCL PLAAYQVSGE YAMILSAFQQ GWLDKETLFH
310 320 330
ESLIAIKRAG ADMIISYSAP FILELLHQGF EF
Length:332
Mass (Da):37,280
Last modified:May 1, 1999 - v1
Checksum:iC29BABFE31114F6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA. Translation: AAD18883.1.
AE002161 Genomic DNA. Translation: AAF37898.1.
BA000008 Genomic DNA. Translation: BAA98951.1.
AE009440 Genomic DNA. Translation: AAP98701.1.
PIRiE86583.
F72040.
RefSeqiNP_224940.1. NC_000922.1.
NP_300800.1. NC_002491.1.
NP_444554.1. NC_002179.2.
NP_877044.1. NC_005043.1.

Genome annotation databases

EnsemblBacteriaiAAD18883; AAD18883; CPn_0744.
AAF37898; AAF37898; CP_0001.
AAP98701; AAP98701; CpB0772.
BAA98951; BAA98951; BAA98951.
GeneIDi895528.
KEGGicpa:CP0001.
cpj:CPj0744.
cpn:CPn0744.
cpt:CpB0772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA. Translation: AAD18883.1.
AE002161 Genomic DNA. Translation: AAF37898.1.
BA000008 Genomic DNA. Translation: BAA98951.1.
AE009440 Genomic DNA. Translation: AAP98701.1.
PIRiE86583.
F72040.
RefSeqiNP_224940.1. NC_000922.1.
NP_300800.1. NC_002491.1.
NP_444554.1. NC_002179.2.
NP_877044.1. NC_005043.1.

3D structure databases

ProteinModelPortaliQ9Z7G1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi115713.CPn0744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD18883; AAD18883; CPn_0744.
AAF37898; AAF37898; CP_0001.
AAP98701; AAP98701; CpB0772.
BAA98951; BAA98951; BAA98951.
GeneIDi895528.
KEGGicpa:CP0001.
cpj:CPj0744.
cpn:CPn0744.
cpt:CpB0772.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciCPNE115711:GI7B-1-MONOMER.
CPNE115713:GHEY-777-MONOMER.
CPNE138677:GH8N-768-MONOMER.
CPNE182082:GH4N-796-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: CWL029.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AR39.
  3. "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
    Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
    Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: J138.
  4. "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
    Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TW-183.

Entry informationi

Entry nameiHEM2_CHLPN
AccessioniPrimary (citable) accession number: Q9Z7G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 98 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.