P78974 (HEM2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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 (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 Reference proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	lead ion binding Inferred from sequence or structural similarity. Source: UniProtKB porphobilinogen synthase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
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	199	1	Schiff-base intermediate with substrate By similarity
	Active site	252	1	Schiff-base intermediate with substrate 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
	Binding site	209	1	Substrate 1 By similarity
	Binding site	221	1	Substrate 1 By similarity
	Binding site	279	1	Substrate 2 By similarity
	Binding site	318	1	Substrate 2 By similarity
Experimental info
	Sequence conflict	60	1	N → H in AAB41236. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P78974 [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: 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.
PIR	T37891.
RefSeq	NP_593917.1. NM_001019346.1.
3D structure databases
ProteinModelPortal	P78974.
SMR	P78974. Positions 4-328.
ModBase	Search...
Protein-protein interaction databases
STRING	P78974.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC1805.06c.1; SPAC1805.06c.1:pep; SPAC1805.06c.
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
eggNOG	fuNOG07497.
GeneTree	EFGT00050000001802.
HOGENOM	HBG285270.
OMA	XDERGSA.
OrthoDB	EOG454D75.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001561-MONOMER.
Gene expression databases
ArrayExpress	P78974.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01698.
PANTHER	PTHR11458. AlaD_dehydratase. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PIRSF	PIRSF001415. Porphbilin_synth. 1 hit.
PRINTS	PR00144. DALDHYDRTASE.
SMART	SM01004. ALAD. 1 hit. [Graphical view]
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:	January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program