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Reviewed, UniProtKB/Swiss-Prot P78974 (HEM2_SCHPO)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
    EC=4.2.1.24
Alternative name(s):
    Porphobilinogen synthase
Gene names
Name: hem2
ORF Names: SPAC1805.06c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Zinc By similarity.

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 processHeme biosynthesis
Porphyrin biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processheme biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionporphobilinogen synthase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Delta-aminolevulinic acid dehydratase
PRO_0000140533

Sites

Active site2521 By similarity
Metal binding1221Zinc; catalytic By similarity
Metal binding1241Zinc; catalytic By similarity
Metal binding1321Zinc; catalytic By similarity

Experimental info

Sequence conflict601N → H in AAB41236. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P78974-1 [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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]Choi J.K., Levin H.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-329.

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAB55847.1.
U83568 mRNA. Translation: AAB41236.1.
PIRT37891.
RefSeqNP_593917.1.

3D structure databases

HSSPHSSP built from PDB template 1E51 based on UniProtKB P13716.
ModBaseSearch...

Protein-protein interaction databases

STRINGP78974.

Genome annotation databases

GeneID2542373.
GenomeReviewsGene locus hem2 in contig CU329670_GR.
KEGGspo:SPAC1805.06c.
NMPDRfig|4896.1.peg.3887.

Organism-specific databases

GeneDB_SpombeSPAC1805.06c.

Phylogenomic databases

OMAGAYLDIL.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001561-MON.
BRENDA4.2.1.24. 653.

Gene expression databases

ArrayExpressP78974.

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_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: November 3, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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