SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P64334

- HEM2_STAAN

UniProt

P64334 - HEM2_STAAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Delta-aminolevulinic acid dehydratase
Gene
hemB, SA1492
Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 bindingi118 – 1181Zinc; catalytic By similarity
Metal bindingi120 – 1201Zinc; catalytic By similarity
Metal bindingi128 – 1281Zinc; 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

BioCyciSAUR158879:GJCB-1565-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:SA1492
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Delta-aminolevulinic acid dehydratase
PRO_0000140512Add
BLAST

Interactioni

Subunit structurei

Homooctamer By similarity.

Protein-protein interaction databases

STRINGi158879.SA1492.

Structurei

3D structure databases

ProteinModelPortaliP64334.
SMRiP64334. Positions 5-318.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALADH family.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OMAiDMILTYF.
OrthoDBiEOG6VXFCB.

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.

P64334-1 [UniParc]FASTAAdd to Basket

« Hide

MKFDRHRRLR SSATMRDMVR ENHVRKEDLI YPIFVVEKDD VKKEIKSLPG    50
VYQISLNLLE SELKEAYDLG IRAIMFFGVP NSKDDIGTGA YIHDGVIQQA 100
TRIAKKMYDD LLIVADTCLC EYTDHGHCGV IDDHTHDVDN DKSLPLLVKT 150
AISQVEAGAD IIAPSNMMDG FVAEIRRGLD EAGYYNIPIM SYGVKYASSF 200
FGPFRDAADS APSFGDRKTY QMDPANRLEA LRELESDLKE GCDMMIVKPA 250
LSYLDIVRDV KNHTNVPVVA YNVSGEYSMT KAAAQNGWID EERVVMEQMV 300
SMKRAGADMI ITYFAKDICR YLDK 324
Length:324
Mass (Da):36,583
Last modified:October 11, 2004 - v1
Checksum:iBF24378E01E7C93E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42759.1.
PIRiB89950.
RefSeqiNP_374780.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42759; BAB42759; BAB42759.
GeneIDi1124337.
KEGGisau:SA1492.
PATRICi19575284. VBIStaAur116463_1612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42759.1 .
PIRi B89950.
RefSeqi NP_374780.1. NC_002745.2.

3D structure databases

ProteinModelPortali P64334.
SMRi P64334. Positions 5-318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA1492.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB42759 ; BAB42759 ; BAB42759 .
GeneIDi 1124337.
KEGGi sau:SA1492.
PATRICi 19575284. VBIStaAur116463_1612.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .
BioCyci SAUR158879:GJCB-1565-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiHEM2_STAAN
AccessioniPrimary (citable) accession number: P64334
Secondary accession number(s): Q99TJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 60 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi