Q60178 (HEM2_METJA) 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:	MJ0643

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	335 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-containing compound 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 – 335	335	Delta-aminolevulinic acid dehydratase		PRO_0000140523
Sites
	Active site	204	1	Schiff-base intermediate with substrate By similarity
	Active site	257	1	Schiff-base intermediate with substrate By similarity
	Metal binding	129	1	Zinc; catalytic By similarity
	Metal binding	131	1	Zinc; catalytic By similarity
	Metal binding	139	1	Zinc; catalytic By similarity
	Metal binding	242	1	Magnesium By similarity
	Binding site	214	1	Substrate 1 By similarity
	Binding site	226	1	Substrate 1 By similarity
	Binding site	283	1	Substrate 2 By similarity
	Binding site	322	1	Substrate 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q60178 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 4D097DAB45F3705D	FASTA	335	37,396
	10 20 30 40 50 60 MFKINLGDFM LIRPRRLRKN QKIRDLVRET ILTKNDLIMP IFVDENLKGN EKKEISSMPN 70 80 90 100 110 120 QYRFSVEGAI EEAKEIADLG IPAVILFGIP KHKDEIASSA YDKNGVVQRT IRGIKEELGD 130 140 150 160 170 180 ELLVIADCCL CEYTSHGHCG IVKDGKILND ATLPILAKIA LSYADAGVDI VAPSDMMDGR 190 200 210 220 230 240 VRAIREILEE NGYDDVAIMS YSAKYASSFY GPFREAAESA PKFGDRKSYQ MDIGNAREAL 250 260 270 280 290 300 KEIALDIEEG ADLILVKPAL PYLDIIRMAK DRFDVPIGGY CVSGEYAMVE AAARNGWLDR 310 320 330 EKVIYEILLS IKRAGADFII TYWAKEVAEI GLSQE

References

[1]

"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB98637.1.
PIR	C64380.
RefSeq	NP_247627.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q60178.
SMR	Q60178. Positions 11-330.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ0643.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB98637; AAB98637; MJ_0643.
GeneID	1451509.
KEGG	mja:MJ_0643.
Phylogenomic databases
eggNOG	COG0113.
KO	K01698.
OMA	DVAIMSY.
ProtClustDB	PRK09283.
Enzyme and pathway databases
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_METJA

Accession

Primary (citable) accession number: Q60178

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program