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P30950

- HEM2_BACSU

UniProt

P30950 - HEM2_BACSU

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Protein
Delta-aminolevulinic acid dehydratase
Gene
hemB, BSU28130
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Binds 1 zinc ion per monomer By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Zinc; catalytic By similarity
Metal bindingi122 – 1221Zinc; catalytic By similarity
Metal bindingi130 – 1301Zinc; catalytic By similarity
Active sitei195 – 1951Schiff-base intermediate with substrate By similarity
Binding sitei205 – 2051Substrate 1 By similarity
Binding sitei217 – 2171Substrate 1 By similarity
Metal bindingi233 – 2331Magnesium By similarity
Active sitei248 – 2481Schiff-base intermediate with substrate By similarity
Binding sitei274 – 2741Substrate 2 By similarity
Binding sitei313 – 3131Substrate 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. porphobilinogen synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU28130-MONOMER.
UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:hemB
Ordered Locus Names:BSU28130
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU28130. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Delta-aminolevulinic acid dehydratase
PRO_0000140493Add
BLAST

Proteomic databases

PaxDbiP30950.

Interactioni

Subunit structurei

Homooctamer By similarity.

Protein-protein interaction databases

STRINGi224308.BSU28130.

Structurei

3D structure databases

ProteinModelPortaliP30950.
SMRiP30950. Positions 5-323.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALADH family.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OMAiDMILTYF.
OrthoDBiEOG6VXFCB.
PhylomeDBiP30950.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30950-1 [UniParc]FASTAAdd to Basket

« Hide

MSQSFNRHRR LRTSKAMREM VKETRLHPSD FIYPIFVVEG LEGKKAVPSM    50
PDVHHVSLDL LKDEVAELVK LGIQSVIVFG IPEEKDDCGT QAYHDHGIVQ 100
KAITEIKEHF PEMVVVADTC LCEYTDHGHC GLVKDGVILN DESLELLAQT 150
AVSQAKAGAD IIAPSNMMDG FVTVIREALD KEGFVNIPIM SYAVKYSSEF 200
YGPFRDAANS TPQFGDRKTY QMDPANRMEA LREAQSDVEE GADFLIVKPS 250
LSYMDIMRDV KNEFTLPLVA YNVSGEYSMV KAAAQNGWIK EKEIVLEILT 300
SMKRAGADLI ITYHAKDAAK WLAE 324
Length:324
Mass (Da):36,209
Last modified:July 1, 1993 - v1
Checksum:iC1CF7E157AE6CB07
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57676 Genomic DNA. Translation: AAA22514.1.
AL009126 Genomic DNA. Translation: CAB14773.1.
PIRiC42728.
RefSeqiNP_390691.1. NC_000964.3.
WP_003229631.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB14773; CAB14773; BSU28130.
GeneIDi936972.
KEGGibsu:BSU28130.
PATRICi18977502. VBIBacSub10457_2940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57676 Genomic DNA. Translation: AAA22514.1 .
AL009126 Genomic DNA. Translation: CAB14773.1 .
PIRi C42728.
RefSeqi NP_390691.1. NC_000964.3.
WP_003229631.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P30950.
SMRi P30950. Positions 5-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU28130.

Proteomic databases

PaxDbi P30950.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14773 ; CAB14773 ; BSU28130 .
GeneIDi 936972.
KEGGi bsu:BSU28130.
PATRICi 18977502. VBIBacSub10457_2940.

Organism-specific databases

GenoListi BSU28130. [Micado ]

Phylogenomic databases

eggNOGi COG0113.
HOGENOMi HOG000020323.
KOi K01698.
OMAi DMILTYF.
OrthoDBi EOG6VXFCB.
PhylomeDBi P30950.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .
BioCyci BSUB:BSU28130-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHEM2_BACSU
AccessioniPrimary (citable) accession number: P30950
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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