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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

Pathway:iprotoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (hemB)
  2. Porphobilinogen deaminase (hemC)
  3. no protein annotated in this organism
  4. Uroporphyrinogen decarboxylase (hemE)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi122 – 1221Zinc; catalyticBy similarity
Metal bindingi124 – 1241Zinc; catalyticBy similarity
Metal bindingi132 – 1321Zinc; catalyticBy similarity
Active sitei197 – 1971Schiff-base intermediate with substrateBy similarity
Binding sitei207 – 2071Substrate 1By similarity
Binding sitei219 – 2191Substrate 1By similarity
Metal bindingi235 – 2351MagnesiumBy similarity
Active sitei250 – 2501Schiff-base intermediate with substrateBy similarity
Binding sitei276 – 2761Substrate 2By similarity
Binding sitei315 – 3151Substrate 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBHAL272558:GJC5-3141-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:BH3044
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Delta-aminolevulinic acid dehydratasePRO_0000140492Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi272558.BH3044.

Structurei

3D structure databases

ProteinModelPortaliQ9K8G2.
SMRiQ9K8G2. Positions 7-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[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.

Q9K8G2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQDLTFKRH RRLRQTAAIR NMVRETKLHI DDLIYPIFVK EGEGVRQEVP
60 70 80 90 100
SMPNVYQLSL DQLDAEVDEI VSLGIPAIIL FGVPAEKDAV GSAAYHEHGI
110 120 130 140 150
VQQAIRQVKE SYPDLTVIAD TCLCQFTDHG HCGVIEEGKI LNDPSLDLLA
160 170 180 190 200
RTAVSQAKAG ADIIAPSNMM DGFVAAIRAG LDSAGFTDVP VMSYAVKYAS
210 220 230 240 250
AFYGPFRDAA HSSPVFGDRK TYQMDPANRL EALREARSDV EEGADFLIVK
260 270 280 290 300
PALSYLDIIR EVKNETGLPV VAYNVSGEYS MIKAASLQGW IDEKSTVLEK
310 320
LISMKRAGAD LILTYFAKDV ARWLNEEK
Length:328
Mass (Da):36,166
Last modified:October 1, 2000 - v1
Checksum:i74BDEEE1C95B1646
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06763.1.
PIRiD84030.
RefSeqiWP_010899188.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB06763; BAB06763; BAB06763.
KEGGibha:BH3044.
PATRICi18943328. VBIBacHal18977_3165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06763.1.
PIRiD84030.
RefSeqiWP_010899188.1. NC_002570.2.

3D structure databases

ProteinModelPortaliQ9K8G2.
SMRiQ9K8G2. Positions 7-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH3044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB06763; BAB06763; BAB06763.
KEGGibha:BH3044.
PATRICi18943328. VBIBacHal18977_3165.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OMAiSTYQMDP.
OrthoDBiEOG6VXFCB.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciBHAL272558:GJC5-3141-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[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]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Entry informationi

Entry nameiHEM2_BACHD
AccessioniPrimary (citable) accession number: Q9K8G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 89 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.