Q59295 (HEM2_CLOJO) 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

Organism

Clostridium josui

Taxonomic identifier

1499 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	205 AA.
Sequence status	Fragment.
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-containing compound 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
Gene Ontology (GO)
Biological_process	protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – ›205	›205	Delta-aminolevulinic acid dehydratase		PRO_0000140500
Sites
	Active site	192	1	Schiff-base intermediate with substrate By similarity
	Metal binding	117	1	Zinc; catalytic By similarity
	Metal binding	119	1	Zinc; catalytic By similarity
	Metal binding	127	1	Zinc; catalytic By similarity
	Binding site	202	1	Substrate By similarity
Experimental info
	Non-terminal residue	205	1

Sequences

	Sequence		Length	Mass (Da)
	Q59295 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 886F9DAEFDB1144E	FASTA	205	23,172
	10 20 30 40 50 60 MIKRPRRLRT NEVLRKAVRE TRLSTDSLIW PLFIVEGKNI KKEISSLPGQ YHFSPDMVGK 70 80 90 100 110 120 AIEAALKADV KSVLLFGLPK HKDEKGSEAY NENGVLQQGI REIKQRYPQM QVITDICMCE 130 140 150 160 170 180 YTSHGHCGIL EGERVDNDRT LPYLEKIALS HVMAGADMIA PSDMMDGRIY ALRSTLDKNG 190 200 FTDIPIMSYA VKYASSFYGP FREAA

References

[1]

"Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui." Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K. J. Bacteriol. 177:5169-5175(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FERM P-9684.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D28503 Genomic DNA. Translation: BAA05863.1.
PIR	I40812.
3D structure databases
ProteinModelPortal	Q59295.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00251; UER00318.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
PANTHER	PTHR11458. PTHR11458. 1 hit.
Pfam	PF00490. ALAD. 1 hit. [Graphical view]
PRINTS	PR00144. DALDHYDRTASE.
SMART	SM01004. ALAD. 1 hit. [Graphical view]
PROSITE	PS00169. D_ALA_DEHYDRATASE. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM2_CLOJO

Accession

Primary (citable) accession number: Q59295

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program