Q02250 (HEM2_METSC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Porphobilinogen synthase

Gene names

Name:	hemB
Synonyms:	alaDH

Organism

Methanothermus sociabilis

Taxonomic identifier

2181 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanothermaceae › Methanothermus

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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	Magnesium Metal-binding Zinc
Molecular function	Lyase
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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
	Chain	1 – 320	320	Delta-aminolevulinic acid dehydratase		PRO_0000140524
Sites
	Active site	194	1	Schiff-base intermediate with substrate By similarity
	Active site	247	1	Schiff-base intermediate with substrate By similarity
	Metal binding	119	1	Zinc; catalytic By similarity
	Metal binding	121	1	Zinc; catalytic By similarity
	Metal binding	129	1	Zinc; catalytic By similarity
	Metal binding	232	1	Magnesium By similarity
	Binding site	204	1	Substrate 1 By similarity
	Binding site	216	1	Substrate 1 By similarity
	Binding site	273	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q02250 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 16F13425105F38D0	FASTA	320	35,925
	10 20 30 40 50 60 MKFPYTRMRR LRKNSKIRSL VKETTLSKDD LIYPVFVKEG IKTKEKIPKM PGQYRYSVDE 70 80 90 100 110 120 LIDEAKKLEE KGLKAILVFG IPKKKDKYGS SAYDPNGIVQ KSVKLLKEET DLVVITDVCL 130 140 150 160 170 180 CQYTEHGHCG IVKNKKIVND ETLKYLSKVA LSHAEAGADV VAPSDMMDGR VKAIREELEK 190 200 210 220 230 240 NGFDDVIIMS YSAKYASSFY EPFRSAVYSS PAFGDRSTYQ MDPPNSLEAL REVKLDIDEG 250 260 270 280 290 300 ADIVMVKPAL PYLDIIRLVK DTFGVPTAAY NVSGEYSMIK AAIDANYLSN KVIIETLLSI 310 320 KRAGADLIIT HFAPEIVEEI

References

[1]	"Sequence of the 5-aminolevulinic acid dehydratase-encoding gene from the hyperthermophilic methanogen, Methanothermus sociabilis." Broeckl G., Berchtold M., Behr M., Koenig H. Gene 119:151-152(1992) [PubMed: 1398086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M90083 Genomic DNA. Translation: AAA73226.1.
PIR	JC1286.
3D structure databases
ProteinModelPortal	Q02250.
SMR	Q02250. Positions 6-319.
ModBase	Search...
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_METSC

Accession

Primary (citable) accession number: Q02250

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program