Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9K8G2 (HEM2_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:BH3044
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceInferred 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 processHeme biosynthesis
Porphyrin biosynthesis
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

porphobilinogen synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Delta-aminolevulinic acid dehydratase
PRO_0000140492

Sites

Active site1971Schiff-base intermediate with substrate By similarity
Active site2501Schiff-base intermediate with substrate By similarity
Metal binding1221Zinc; catalytic By similarity
Metal binding1241Zinc; catalytic By similarity
Metal binding1321Zinc; catalytic By similarity
Metal binding2351Magnesium By similarity
Binding site2071Substrate 1 By similarity
Binding site2191Substrate 1 By similarity
Binding site2761Substrate 2 By similarity
Binding site3151Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K8G2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 74BDEEE1C95B1646

FASTA32836,166
        10         20         30         40         50         60 
MGQDLTFKRH RRLRQTAAIR NMVRETKLHI DDLIYPIFVK EGEGVRQEVP SMPNVYQLSL 

        70         80         90        100        110        120 
DQLDAEVDEI VSLGIPAIIL FGVPAEKDAV GSAAYHEHGI VQQAIRQVKE SYPDLTVIAD 

       130        140        150        160        170        180 
TCLCQFTDHG HCGVIEEGKI LNDPSLDLLA RTAVSQAKAG ADIIAPSNMM DGFVAAIRAG 

       190        200        210        220        230        240 
LDSAGFTDVP VMSYAVKYAS AFYGPFRDAA HSSPVFGDRK TYQMDPANRL EALREARSDV 

       250        260        270        280        290        300 
EEGADFLIVK PALSYLDIIR EVKNETGLPV VAYNVSGEYS MIKAASLQGW IDEKSTVLEK 

       310        320 
LISMKRAGAD LILTYFAKDV ARWLNEEK 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06763.1.
PIRD84030.
RefSeqNP_243910.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K8G2.
SMRQ9K8G2. Positions 7-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH3044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB06763; BAB06763; BAB06763.
GeneID890913.
KEGGbha:BH3044.
PATRIC18943328. VBIBacHal18977_3165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAGEYAMVE.
OrthoDBEOG6VXFCB.
ProtClustDBPRK09283.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-3141-MONOMER.
UniPathwayUPA00251; UER00318.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_BACHD
AccessionPrimary (citable) accession number: Q9K8G2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: November 13, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways