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P30950 (HEM2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:BSU28130
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length324 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 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
Reference 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324Delta-aminolevulinic acid dehydratase
PRO_0000140493

Sites

Active site1951Schiff-base intermediate with substrate By similarity
Active site2481Schiff-base intermediate with substrate By similarity
Metal binding1201Zinc; catalytic By similarity
Metal binding1221Zinc; catalytic By similarity
Metal binding1301Zinc; catalytic By similarity
Metal binding2331Magnesium By similarity
Binding site2051Substrate 1 By similarity
Binding site2171Substrate 1 By similarity
Binding site2741Substrate 2 By similarity
Binding site3131Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P30950 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: C1CF7E157AE6CB07

FASTA32436,209
        10         20         30         40         50         60 
MSQSFNRHRR LRTSKAMREM VKETRLHPSD FIYPIFVVEG LEGKKAVPSM PDVHHVSLDL 

        70         80         90        100        110        120 
LKDEVAELVK LGIQSVIVFG IPEEKDDCGT QAYHDHGIVQ KAITEIKEHF PEMVVVADTC 

       130        140        150        160        170        180 
LCEYTDHGHC GLVKDGVILN DESLELLAQT AVSQAKAGAD IIAPSNMMDG FVTVIREALD 

       190        200        210        220        230        240 
KEGFVNIPIM SYAVKYSSEF YGPFRDAANS TPQFGDRKTY QMDPANRMEA LREAQSDVEE 

       250        260        270        280        290        300 
GADFLIVKPS LSYMDIMRDV KNEFTLPLVA YNVSGEYSMV KAAAQNGWIK EKEIVLEILT 

       310        320 
SMKRAGADLI ITYHAKDAAK WLAE

« Hide

References

« Hide 'large scale' references
[1]"The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III."
Hansson M., Rutberg L., Schroeder I., Hederstedt L.
J. Bacteriol. 173:2590-2599(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M57676 Genomic DNA. Translation: AAA22514.1.
AL009126 Genomic DNA. Translation: CAB14773.1.
PIRC42728.
RefSeqNP_390691.1. NC_000964.3.

3D structure databases

ProteinModelPortalP30950.
SMRP30950. Positions 5-323.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU28130.

Proteomic databases

PaxDbP30950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14773; CAB14773; BSU28130.
GeneID936972.
KEGGbsu:BSU28130.
PATRIC18977502. VBIBacSub10457_2940.

Organism-specific databases

GenoListBSU28130. [Micado]

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAMIISYHA.
ProtClustDBPRK09283.

Enzyme and pathway databases

BioCycBSUB:BSU28130-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_BACSU
AccessionPrimary (citable) accession number: P30950
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents