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.

O28305

- HEM2_ARCFU

UniProt

O28305 - HEM2_ARCFU

(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, AF_1974
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
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 sitei312 – 3121Substrate 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

BioCyciAFUL224325:GJBC-2011-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:AF_1974
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Delta-aminolevulinic acid dehydratasePRO_0000140522Add
BLAST

Interactioni

Subunit structurei

Homooctamer By similarity.

Protein-protein interaction databases

STRINGi224325.AF1974.

Structurei

3D structure databases

ProteinModelPortaliO28305.
SMRiO28305. Positions 6-320.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALADH family.

Phylogenomic databases

eggNOGiCOG0113.
KOiK01698.
OMAiDMILTYF.

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.

O28305-1 [UniParc]FASTAAdd to Basket

« Hide

MAEFPKVRMR RLRKANLRWM FREARLSPEN LITPIFVDEN IKEKKPIESM    50
PDYFRIPLEM VDKEVEECLE KDLRSFILFG IPSYKDETGS SAYDQNGVIQ 100
KAVRRIKAEF PDAVIVTDVC LCEYTTHGHC GVVKDGEIVN DETLPIIGKT 150
AVSHAESGAD IVAPSGMMDG MVKAIREALD AAGFESTPIM SYSAKYASNF 200
YSPFRDAAES GFKFGDRRGY QMDIHNAREA MREIELDVKE GADIIMVKPA 250
LPYLDIIRMV RERFDLPLAA YNVSGEYSMI KAAIKNGWLS EEAIYEVLIS 300
IKRAGADLII TYHSKEIAEK LQ 322
Length:322
Mass (Da):36,398
Last modified:January 1, 1998 - v1
Checksum:i5FE684E6B394B509
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000782 Genomic DNA. Translation: AAB89292.1.
PIRiE69496.
RefSeqiNP_070798.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89292; AAB89292; AF_1974.
GeneIDi1485196.
KEGGiafu:AF1974.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000782 Genomic DNA. Translation: AAB89292.1 .
PIRi E69496.
RefSeqi NP_070798.1. NC_000917.1.

3D structure databases

ProteinModelPortali O28305.
SMRi O28305. Positions 6-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224325.AF1974.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB89292 ; AAB89292 ; AF_1974 .
GeneIDi 1485196.
KEGGi afu:AF1974.

Phylogenomic databases

eggNOGi COG0113.
KOi K01698.
OMAi DMILTYF.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .
BioCyci AFUL224325:GJBC-2011-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. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Entry informationi

Entry nameiHEM2_ARCFU
AccessioniPrimary (citable) accession number: O28305
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 86 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