Q8KCJ0 (HEM2_CHLTE) 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
Ordered Locus Names:	CT1431

Organism

Chlorobium tepidum

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	328 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.
Enzyme regulation	Stimulated by magnesium, inhibited by zinc.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer By similarity.
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
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
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 – 328	328	Delta-aminolevulinic acid dehydratase		PRO_0000140497
Sites
	Active site	200	1	Schiff-base intermediate with substrate By similarity
	Active site	253	1	Schiff-base intermediate with substrate By similarity
	Metal binding	238	1	Magnesium By similarity
	Binding site	210	1	Substrate 1 By similarity
	Binding site	222	1	Substrate 1 By similarity
	Binding site	279	1	Substrate 2 By similarity
	Binding site	318	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8KCJ0 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 55556CA0D0632148	FASTA	328	36,433
	10 20 30 40 50 60 MSQLDLLNIV HRPRRLRRTA ALRNLVQENT LTVNDLVFPL FVMPGTNAVE EVPSMPGSFR 70 80 90 100 110 120 FTIDRAVEEC KELYDLGIQA IDLFGIPEKK TEDGSEAYND NGILQQAIRA IKKAVPELCI 130 140 150 160 170 180 MTDVALDPFT PFGHDGLVRD GIILNDETVE VLQKMAVSHA EAGADFVSPS DMMDGRIGAI 190 200 210 220 230 240 REALDESDHS DVGILSYAAK YASSFYGPFR DALHSAPQFG DKSTYQMNPA NTDEAMKEVE 250 260 270 280 290 300 LDIIEGADIV MVKPGLAYLD IVWRTKERFD VPVAIYHVSG EYAMVKAAAA NGWIDEERVM 310 320 MESLLCMKRA GADIIFTYYA KEAAKKLR

References

[1]

"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006470 Genomic DNA. Translation: AAM72659.1.
RefSeq	NP_662317.1. NC_002932.3.
3D structure databases
ProteinModelPortal	Q8KCJ0.
SMR	Q8KCJ0. Positions 10-328.
ModBase	Search...
Proteomic databases
PRIDE	Q8KCJ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1005979.
GenomeReviews	Gene locus CT1431 in contig AE006470_GR.
KEGG	cte:CT1431.
NMPDR	fig|194439.1.peg.1411.
PATRIC	21400789. VBIChlTep116050_1299.
TIGR	CT1431.
Phylogenomic databases
HOGENOM	HBG285270.
OMA	FTSHGHD.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_1431-MONOMER.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR001731. Porphobilinogen_synth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01698.
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_CHLTE

Accession

Primary (citable) accession number: Q8KCJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program