Q9PLU4 (HEM2_CHLMU) 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:	TC_0001

Organism

Chlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]

Taxonomic identifier

243161 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chlamydiae/Verrucomicrobia group › Chlamydiae › Chlamydiia › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › Chlamydia muridarum

Protein attributes

Sequence length	333 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.
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
Molecular function	Lyase
Technical term	Complete proteome
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 – 333	333	Delta-aminolevulinic acid dehydratase		PRO_0000140495
Sites
	Active site	199	1	Schiff-base intermediate with substrate By similarity
	Active site	252	1	Schiff-base intermediate with substrate By similarity
	Metal binding	237	1	Magnesium By similarity
	Binding site	209	1	Substrate 1 By similarity
	Binding site	221	1	Substrate 1 By similarity
	Binding site	278	1	Substrate 2 By similarity
	Binding site	317	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PLU4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 905DC8BCE50B87B5	FASTA	333	37,450
	10 20 30 40 50 60 MTRLPLLKRP RRNRKSAAIR SMIRETNMVS SDLIWPIFLK EGSGIREEIP SMPGVYRWSL 70 80 90 100 110 120 DTISRELERL CLIGLKAVIL FPVIEDQKKD QFGAYASHPY NIVCRGIQEI KKSFPQLCVI 130 140 150 160 170 180 SDIALDPFTT SGHDGIFYNN EVLNDESVRV YGDIATLHAE MGADIVAPSD MMDGRVRHIR 190 200 210 220 230 240 EKMDQMGFVN TGILSYSAKY ASYLYGPFRD ALSSHPQSGD KRQYQMDPAN VREALLECRL 250 260 270 280 290 300 DEEEGADMVM IKPAGFYLDV IMKAQECTHL PVVAYQVSGE YSMIMAASLH GWLSKEGAIS 310 320 330 ESLLAIKRAG ATAIISYATP WVLEWLARDA LPF

References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF38895.1.
PIR	B81751.
RefSeq	NP_296385.1. NC_002620.2.
3D structure databases
ProteinModelPortal	Q9PLU4.
ModBase	Search...
Protein-protein interaction databases
STRING	243161.TC0001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF38895; AAF38895; TC_0001.
GeneID	1245524.
KEGG	cmu:TC0001.
PATRIC	20371336. VBIChlMur19118_0011.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0113.
KO	K01698.
OMA	DVAIMSY.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	CMUR243161:GHYU-2-MONOMER.
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]
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_CHLMU

Accession

Primary (citable) accession number: Q9PLU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program