Q42682 (HEM2_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta-aminolevulinic acid dehydratase, chloroplastic
Short name=ALADH
EC=4.2.1.24

Alternative name(s):
Porphobilinogen synthase

Gene names

Name:	HEMB
Synonyms:	ALAD

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer By similarity.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the ALADH family.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Heme biosynthesis Porphyrin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW porphobilinogen synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 24	24	Chloroplast Potential
	Chain	25 – 390	366	Delta-aminolevulinic acid dehydratase, chloroplastic		PRO_0000013315
Sites
	Active site	251	1	Schiff-base intermediate with substrate By similarity
	Active site	312	1	Schiff-base intermediate with substrate By similarity
	Metal binding	297	1	Magnesium By similarity
	Binding site	261	1	Substrate 1 By similarity
	Binding site	281	1	Substrate 1 By similarity
	Binding site	338	1	Substrate 2 By similarity
	Binding site	377	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q42682 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 6114C4E0325A4242	FASTA	390	43,046
	10 20 30 40 50 60 MQMMQRNVVG QRPVAGSRRS LVVANVAEVT RPAVSTNGKH RTGVPEGTPI VTPQDLPSRP 70 80 90 100 110 120 RRNRRSESFR ASVREVNVSP ANFILPIFIH EESNQNVPIA SMPGINRLAY GKNVIDYVAE 130 140 150 160 170 180 PRSYGVNQVV VFPKTPDHLK TQTAEEAFNK NGLSQRTIRL LKDSFPDLEV YTDVALDPYN 190 200 210 220 230 240 SDGHDGIVSD AGVILNDETI EYLCRQAVSQ AEAGADVVSP SDMMDGRVGA IRRALDREGF 250 260 270 280 290 300 TNVSIMSYTA KYASAYYGPF RDALASAPKP GQAHRRIPPN KKTYQMDPAN YREAIREAKA 310 320 330 340 350 360 DEAEGADIMM VKPGMPYLDV VRLLRETSPL PVAVYHVSGE YAMLKAAAER GWLNEKDAVL 370 380 390 EAMTCFRRAG GDLILTYYGI EASKWLAGEK

References

[1]	"Structure and expression of the Chlamydomonas reinhardtii alad gene encoding the chlorophyll biosynthetic enzyme, delta-aminolevulinic acid dehydratase (porphobilinogen synthase)." Matters G.L., Beale S.I. Plant Mol. Biol. 27:607-617(1995) [PubMed: 7894023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: NO-.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U19876 mRNA. Translation: AAA79515.1.
PIR	S53487.
3D structure databases
ProteinModelPortal	Q42682.
SMR	Q42682. Positions 58-387.
ModBase	Search...
Protein-protein interaction databases
STRING	Q42682.
Proteomic databases
PRIDE	Q42682.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [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.
SMART	SM01004. ALAD. 1 hit. [Graphical view]
PROSITE	PS00169. D_ALA_DEHYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM2_CHLRE

Accession

Primary (citable) accession number: Q42682

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program