Reviewed, UniProtKB/Swiss-Prot P78974 (HEM2_SCHPO)

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Heme biosynthesis Porphyrin biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	porphobilinogen 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Delta-aminolevulinic acid dehydratase		PRO_0000140533
Sites
	Active site	252	1	By similarity
	Metal binding	122	1	Zinc; catalytic By similarity
	Metal binding	124	1	Zinc; catalytic By similarity
	Metal binding	132	1	Zinc; catalytic By similarity
Experimental info
	Sequence conflict	60	1	N → H in AAB41236. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P78974-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: A4BFA966C3C83F60	FASTA	329	36,121
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB55847.1. U83568 mRNA. Translation: AAB41236.1.
PIR	T37891.
RefSeq	NP_593917.1.
3D structure databases
HSSP	HSSP built from PDB template 1E51 based on UniProtKB P13716.
ModBase	Search...
Protein-protein interaction databases
STRING	P78974.
Genome annotation databases
GeneID	2542373.
GenomeReviews	Gene locus hem2 in contig CU329670_GR.
KEGG	spo:SPAC1805.06c.
NMPDR	fig|4896.1.peg.3887.
Organism-specific databases
GeneDB_Spombe	SPAC1805.06c.
Phylogenomic databases
OMA	GAYLDIL.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001561-MON.
BRENDA	4.2.1.24. 653.
Gene expression databases
ArrayExpress	P78974.
Family and domain databases
InterPro	IPR001731. 4pyrrol_synth_porphobiln_synth. IPR013785. Aldolase_TIM. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PIRSF	PIRSF001415. Porphbilin_synth. 1 hit.
PRINTS	PR00144. DALDHYDRTASE.
ProDom	PD002304. AlaD_dehydratase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM2_SCHPO

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)