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Protein

Delta-aminolevulinic acid dehydratase

Gene

hem2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

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 (hem2)
  2. Porphobilinogen deaminase (hem3)
  3. Uroporphyrinogen-III synthase (ups1)
  4. Uroporphyrinogen decarboxylase (hem12)
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
Metal bindingi122 – 1221Zinc; catalyticBy similarity
Metal bindingi124 – 1241Zinc; catalyticBy similarity
Metal bindingi132 – 1321Zinc; catalyticBy similarity
Active sitei199 – 1991Schiff-base intermediate with substrateBy similarity
Binding sitei209 – 2091Substrate 1By similarity
Binding sitei221 – 2211Substrate 1By similarity
Active sitei252 – 2521Schiff-base intermediate with substrateBy similarity
Binding sitei279 – 2791Substrate 2By similarity
Binding sitei318 – 3181Substrate 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_327500. Heme biosynthesis.
UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:hem2
ORF Names:SPAC1805.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1805.06c.
PomBaseiSPAC1805.06c. hem2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Delta-aminolevulinic acid dehydratasePRO_0000140533Add
BLAST

Proteomic databases

MaxQBiP78974.
PaxDbiP78974.

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

BioGridi278837. 8 interactions.
MINTiMINT-4691801.
STRINGi4896.SPAC1805.06c.1.

Structurei

3D structure databases

ProteinModelPortaliP78974.
SMRiP78974. Positions 4-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiP78974.
KOiK01698.
OMAiADCIITY.
OrthoDBiEOG779P7W.
PhylomeDBiP78974.

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.

P78974-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVDISSLLH AGYSNPLLRE WQGVRPITKS SLMYPIFISE IDDAKEAIDS
60 70 80 90 100
MPNQFRWGVN RLEEFLGPLV KKGLRSVILF GVIESKKDYC GSMADSENGP
110 120 130 140 150
VIKAVKEIRH LFPELVVACD VCLCEYTDHG HCGLLYEDGT INNAKSVERI
160 170 180 190 200
AEVSGNYALA GAQIISPSDC MDGRVKAIKQ KLVELELSHK VCVISYSAKF
210 220 230 240 250
ASGFFGPFRA AANGAPKFGD RSCYQLPCNA RGLAKRAILR DVREGADGIM
260 270 280 290 300
VKPGTPYLDI LAMASKLADD LPIATYQVSG EFAIIHAAAA AGVFELKRHV
310 320
METMDGFMRA GANIVLTYFT PELLEWLEY
Length:329
Mass (Da):36,121
Last modified:December 1, 2000 - v2
Checksum:iA4BFA966C3C83F60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601N → H in AAB41236 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB55847.1.
U83568 mRNA. Translation: AAB41236.1.
PIRiT37891.
RefSeqiNP_593917.1. NM_001019346.2.

Genome annotation databases

EnsemblFungiiSPAC1805.06c.1; SPAC1805.06c.1:pep; SPAC1805.06c.
GeneIDi2542373.
KEGGispo:SPAC1805.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB55847.1.
U83568 mRNA. Translation: AAB41236.1.
PIRiT37891.
RefSeqiNP_593917.1. NM_001019346.2.

3D structure databases

ProteinModelPortaliP78974.
SMRiP78974. Positions 4-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278837. 8 interactions.
MINTiMINT-4691801.
STRINGi4896.SPAC1805.06c.1.

Proteomic databases

MaxQBiP78974.
PaxDbiP78974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1805.06c.1; SPAC1805.06c.1:pep; SPAC1805.06c.
GeneIDi2542373.
KEGGispo:SPAC1805.06c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1805.06c.
PomBaseiSPAC1805.06c. hem2.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiP78974.
KOiK01698.
OMAiADCIITY.
OrthoDBiEOG779P7W.
PhylomeDBiP78974.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
ReactomeiREACT_327500. Heme biosynthesis.

Miscellaneous databases

NextBioi20803432.
PROiP78974.

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

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHEM2_SCHPO
AccessioniPrimary (citable) accession number: P78974
Secondary accession number(s): Q9UTG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 1, 2000
Last modified: June 24, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.