P42504 (HEM2_RHOCA) 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

Rhodobacter capsulatus (Rhodopseudomonas capsulata)

Taxonomic identifier

1061 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.2
Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O. Ref.2
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homohexamer. Ref.2
Miscellaneous	Does not seem to have a metal requirement for activity.
Sequence similarities	Belongs to the ALADH family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
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: InterPro 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 – 332	332	Delta-aminolevulinic acid dehydratase		PRO_0000140508
Sites
	Active site	202	1	Schiff-base intermediate with substrate By similarity
	Active site	256	1	Schiff-base intermediate with substrate By similarity
	Binding site	212	1	Substrate 1 By similarity
	Binding site	225	1	Substrate 1 By similarity
	Binding site	282	1	Substrate 2 By similarity
	Binding site	321	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42504 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4118DED5A15C8DBE	FASTA	332	35,854
	10 20 30 40 50 60 MTLITPPFPT NRLRRMRRTE ALRDLAQENR LSVKDLIWPI FITDVPGADV EISSMPGVVR 70 80 90 100 110 120 RTMDGALKAA EGSRDAGHSR DLPVPLTDPA VKTETCEMAW QPDNFTNRVI AAMKQAVPEV 130 140 150 160 170 180 AIMTDIALDP YNANGHDGLV RDGILLNDET TEALVKMALA QAAAGADILG PSDMMDGRVG 190 200 210 220 230 240 AIRQAMEAAG HKDIAILSYA AKYASAFYGP FRDAVGASSA LKGDKKTYQM NPANSAEALR 250 260 270 280 290 300 NVARDIAEGA DMVMVKPGMP YLDIVRQVKD AFGMPTYAYQ VSGEYAMLMA AVQNGWLNHD 310 320 330 KVMLESLMAF RRAGCDGVLT YFAPAAAKLI GA

References

[1]	"Nucleotide sequence of the Rhodobacter capsulatus hemB gene." Indest K., Biel A.J. Plant Physiol. 108:421-421(1995) [PubMed: 7784513] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PAS100.
[2]	"Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer." Bollivar D.W., Clauson C., Lighthall R., Forbes S., Kokona B., Fairman R., Kundrat L., Jaffe E.K. BMC Biochem. 5:17-17(2004) [PubMed: 15555082] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION, ABSENCE OF METAL COFACTOR REQUIREMENT, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14593 Genomic DNA. Translation: AAA92884.1.
3D structure databases
ProteinModelPortal	P42504.
SMR	P42504. Positions 8-331.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13250.
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_RHOCA

Accession

Primary (citable) accession number: P42504

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program