Reviewed, UniProtKB/Swiss-Prot Q59295 (HEM2_CLOJO)

Names and origin

Protein names

Recommended name:
    Delta-aminolevulinic acid dehydratase
      Short name=ALADH
      Short name=ALAD
    EC=4.2.1.24
Alternative name(s):
    Porphobilinogen synthase

Gene names

Name:

hemB

Organism

Clostridium josui

Taxonomic identifier

1499 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	205 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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	Porphyrin biosynthesis
Ligand	Zinc
Molecular function	Lyase
Gene Ontology (GO)
Biological process	porphyrin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – ›205	›205	Delta-aminolevulinic acid dehydratase		PRO_0000140500
Regions
	Region	114 – 132	19	Zinc-binding By similarity
Experimental info
	Non-terminal residue	205	1

Sequences

	Sequence		Length	Mass (Da)
	Q59295-1 [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: 7665501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FERM P-9684.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D28503 Genomic DNA. Translation: BAA05863.1.
PIR	I40812.
3D structure databases
HSSP	HSSP built from PDB template 1L6S based on UniProtKB P15002.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.24. 257917.
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]
PRINTS	PR00144. DALDHYDRTASE.
ProDom	PD002304. AlaD_dehydratase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)