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.

Q2FXR3

- HEM2_STAA8

UniProt

Q2FXR3 - HEM2_STAA8

(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, SAOUHSC_01772
Organism
Staphylococcus aureus (strain NCTC 8325)
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 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
Complete GO annotation...

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

BioCyciSAUR93061:GIWJ-1691-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:SAOUHSC_01772
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000008816: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Delta-aminolevulinic acid dehydratase
PRO_0000247939Add
BLAST

Interactioni

Subunit structurei

Homooctamer By similarity.

Protein-protein interaction databases

STRINGi93061.SAOUHSC_01772.

Structurei

3D structure databases

ProteinModelPortaliQ2FXR3.
SMRiQ2FXR3. 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.

Q2FXR3-1 [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:March 21, 2006 - v1
Checksum:iBF24378E01E7C93E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti314 – 3152FA → C in AAC45835. 1 Publication
Sequence conflicti324 – 3241K → N in AAC45835. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U89396 Genomic DNA. Translation: AAC45835.1.
CP000253 Genomic DNA. Translation: ABD30841.1.
RefSeqiYP_500277.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD30841; ABD30841; SAOUHSC_01772.
GeneIDi3919690.
KEGGisao:SAOUHSC_01772.
PATRICi19580911. VBIStaAur99865_1616.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U89396 Genomic DNA. Translation: AAC45835.1 .
CP000253 Genomic DNA. Translation: ABD30841.1 .
RefSeqi YP_500277.1. NC_007795.1.

3D structure databases

ProteinModelPortali Q2FXR3.
SMRi Q2FXR3. Positions 5-318.
ModBasei Search...

Protein-protein interaction databases

STRINGi 93061.SAOUHSC_01772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD30841 ; ABD30841 ; SAOUHSC_01772 .
GeneIDi 3919690.
KEGGi sao:SAOUHSC_01772.
PATRICi 19580911. VBIStaAur99865_1616.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .
BioCyci SAUR93061:GIWJ-1691-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. "Isolation of the Staphylococcus aureus hemCDBL gene cluster coding for early steps in heme biosynthesis."
    Kafala B., Sasarman A.
    Gene 199:231-239(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The Staphylococcus aureus NCTC 8325 genome."
    Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
    (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 8325.

Entry informationi

Entry nameiHEM2_STAA8
AccessioniPrimary (citable) accession number: Q2FXR3
Secondary accession number(s): P50915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 58 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi