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Reviewed, UniProtKB/Swiss-Prot P30950 (HEM2_BACSU)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Delta-aminolevulinic acid dehydratase
      Short name=ALADH
      Short name=ALAD
    EC=4.2.1.24
Alternative name(s):
    Porphobilinogen synthase
Gene names
Name: hemB
Ordered Locus Names: BSU28130
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Zinc 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.

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Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandZinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processporphyrin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionporphobilinogen synthase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324Delta-aminolevulinic acid dehydratase
PRO_0000140493

Regions

Region117 – 13519Zinc-binding By similarity

Sites

Active site2481 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P30950-1 [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

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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: 1672867] [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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

M57676 Genomic DNA. Translation: AAA22514.1.
AL009126 Genomic DNA. Translation: CAB14773.1.
PIRC42728.
RefSeqNP_390691.1.

3D structure databases

HSSPHSSP built from PDB template 1B4K based on UniProtKB Q59643.
ModBaseSearch...

Genome annotation databases

GeneID936972.
GenomeReviewsGene locus BSU28130 in contig AL009126_GR.
KEGGbsu:BSU28130.
NMPDRfig|224308.1.peg.2816.

Organism-specific databases

SubtiListBG10344. hemB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP30950.
OMAP30950. AESTPQF.

Enzyme and pathway databases

BioCycBSUB224308:BSU2809-MON.
BRENDA4.2.1.24. 150.

Family and domain databases

InterProIPR001731. 4pyrrol_synth_porphobiln_synth.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11458. AlaD_dehydratase. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
ProDomPD002304. AlaD_dehydratase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents