O28305 (HEM2_ARCFU) 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:	AF_1974

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus › Archaeoglobus fulgidus

Protein attributes

Sequence length	322 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.
Cofactor	Binds 1 zinc ion per monomer 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	Heme biosynthesis Porphyrin biosynthesis
Ligand	Magnesium Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference 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 – 322	322	Delta-aminolevulinic acid dehydratase		PRO_0000140522
Sites
	Active site	195	1	Schiff-base intermediate with substrate By similarity
	Active site	248	1	Schiff-base intermediate with substrate By similarity
	Metal binding	120	1	Zinc; catalytic By similarity
	Metal binding	122	1	Zinc; catalytic By similarity
	Metal binding	130	1	Zinc; catalytic By similarity
	Metal binding	233	1	Magnesium By similarity
	Binding site	205	1	Substrate 1 By similarity
	Binding site	217	1	Substrate 1 By similarity
	Binding site	274	1	Substrate 2 By similarity
	Binding site	312	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O28305 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 5FE684E6B394B509	FASTA	322	36,398
	10 20 30 40 50 60 MAEFPKVRMR RLRKANLRWM FREARLSPEN LITPIFVDEN IKEKKPIESM PDYFRIPLEM 70 80 90 100 110 120 VDKEVEECLE KDLRSFILFG IPSYKDETGS SAYDQNGVIQ KAVRRIKAEF PDAVIVTDVC 130 140 150 160 170 180 LCEYTTHGHC GVVKDGEIVN DETLPIIGKT AVSHAESGAD IVAPSGMMDG MVKAIREALD 190 200 210 220 230 240 AAGFESTPIM SYSAKYASNF YSPFRDAAES GFKFGDRRGY QMDIHNAREA MREIELDVKE 250 260 270 280 290 300 GADIIMVKPA LPYLDIIRMV RERFDLPLAA YNVSGEYSMI KAAIKNGWLS EEAIYEVLIS 310 320 IKRAGADLII TYHSKEIAEK LQ

References

[1]

"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB89292.1.
PIR	E69496.
RefSeq	NP_070798.1. NC_000917.1.
3D structure databases
ProteinModelPortal	O28305.
SMR	O28305. Positions 6-320.
ModBase	Search...
Protein-protein interaction databases
STRING	224325.AF1974.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB89292; AAB89292; AF_1974.
GeneID	1485196.
KEGG	afu:AF1974.
Phylogenomic databases
eggNOG	COG0113.
KO	K01698.
OMA	DVAIMSY.
ProtClustDB	PRK09283.
Enzyme and pathway databases
BioCyc	AFUL224325:GJBC-2011-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_ARCFU

Accession

Primary (citable) accession number: O28305

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program