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P78974 (HEM2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:hem2
ORF Names:SPAC1805.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length329 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 1 zinc ion per monomer By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Delta-aminolevulinic acid dehydratase
PRO_0000140533

Sites

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

Experimental info

Sequence conflict601N → H in AAB41236. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P78974 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: A4BFA966C3C83F60

FASTA32936,121
        10         20         30         40         50         60 
MPVDISSLLH AGYSNPLLRE WQGVRPITKS SLMYPIFISE IDDAKEAIDS MPNQFRWGVN 

        70         80         90        100        110        120 
RLEEFLGPLV KKGLRSVILF GVIESKKDYC GSMADSENGP VIKAVKEIRH LFPELVVACD 

       130        140        150        160        170        180 
VCLCEYTDHG HCGLLYEDGT INNAKSVERI AEVSGNYALA GAQIISPSDC MDGRVKAIKQ 

       190        200        210        220        230        240 
KLVELELSHK VCVISYSAKF ASGFFGPFRA AANGAPKFGD RSCYQLPCNA RGLAKRAILR 

       250        260        270        280        290        300 
DVREGADGIM VKPGTPYLDI LAMASKLADD LPIATYQVSG EFAIIHAAAA AGVFELKRHV 

       310        320 
METMDGFMRA GANIVLTYFT PELLEWLEY 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]Choi J.K., Levin H.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-329.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB55847.1.
U83568 mRNA. Translation: AAB41236.1.
PIRT37891.
RefSeqNP_593917.1. NM_001019346.2.

3D structure databases

ProteinModelPortalP78974.
SMRP78974. Positions 4-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278837. 7 interactions.
MINTMINT-4691801.
STRING4896.SPAC1805.06c-1.

Proteomic databases

PaxDbP78974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1805.06c.1; SPAC1805.06c.1:pep; SPAC1805.06c.
GeneID2542373.
KEGGspo:SPAC1805.06c.

Organism-specific databases

PomBaseSPAC1805.06c.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAIITYFTP.
OrthoDBEOG779P7W.
PhylomeDBP78974.

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...

Other

NextBio20803432.
PROP78974.

Entry information

Entry nameHEM2_SCHPO
AccessionPrimary (citable) accession number: P78974
Secondary accession number(s): Q9UTG9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways