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Q60HH9 (HEM2_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 41. 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=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:ALAD
ORF Names:QorA-10240
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Cofactor

Binds 8 zinc ions per octamer. Only four zinc ions per octamer are required for full catalytic activity. Only four zinc ions per octamer are tightly bound. Can bind 2 zinc ions per subunit. The first zinc ion is important for catalysis By similarity.

Enzyme regulation

Can alternate between a fully active homooctamer and a low-activity homohexamer. A bound magnesium ion may promote the assembly of the fully active homooctamer. The magnesium-binding site is absent in the low-activity homohexamer. Inhibited by compounds that favor the hexameric state. Inhibited by divalent lead ions. The lead ions partially displace the zinc cofactor By similarity.

Pathway

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

Subunit structure

Homooctamer; active form. Homohexamer; low activity form By similarity.

Sequence similarities

Belongs to the ALADH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Delta-aminolevulinic acid dehydratase
PRO_0000140527

Sites

Active site1991Schiff-base intermediate with substrate By similarity
Active site2521Schiff-base intermediate with substrate By similarity
Metal binding1221Zinc 1; catalytic By similarity
Metal binding1241Zinc 1; catalytic By similarity
Metal binding1311Zinc 2 By similarity
Metal binding1321Zinc 1; catalytic By similarity
Metal binding2231Zinc 2 By similarity
Binding site2091Substrate 1 By similarity
Binding site2211Substrate 1 By similarity
Binding site2791Substrate 2 By similarity
Binding site3181Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60HH9 [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: 70527006BE58BEAA

FASTA33036,246
        10         20         30         40         50         60 
MQPQSVLHSG YFHPLLRAWQ TATTTLNASN LIYPIFVTDV PDDIQPIASL PGVARYGVNR 

        70         80         90        100        110        120 
LEEMLRPLVE EGLRCVLIFG IPSRVPKDER GSAADSEESP AIEAIHLLRK TFPNLLVACD 

       130        140        150        160        170        180 
ICLCPYTSHG HCGLLSENGA FRAEESRQRL AEVALAYAKA GCQVVAPSDM MDGRVEAIKE 

       190        200        210        220        230        240 
ALMAHGLGNR VSVMSYSAKF ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVDR 

       250        260        270        280        290        300 
DVREGADVLM VKPGMPYLDI VREVKDKHPD LPLAVYHVSG EFAMLWHGAQ AGAFDLKAAV 

       310        320        330 
LEAMTAFRRA GADIIITYYT PQLLQWLKKE

« Hide

References

[1]"Isolation and characterization of cDNA for macaque neurological disease genes."
Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Occipital cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB125148 mRNA. Translation: BAD51936.1. Sequence problems.

3D structure databases

ProteinModelPortalQ60HH9.
SMRQ60HH9. Positions 1-328.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001222.

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_MACFA
AccessionPrimary (citable) accession number: Q60HH9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: March 6, 2013
This is version 41 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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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