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Protein

Delta-aminolevulinic acid dehydratase

Gene

hemB

Organism
Propionibacterium freudenreichii subsp. freudenreichii
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.

Pathway: protoporphyrin-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. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (hemE), Uroporphyrinogen decarboxylase (RM25_1803)
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
Active sitei201 – 2011Schiff-base intermediate with substrateBy similarity
Binding sitei211 – 2111Substrate 1By similarity
Binding sitei222 – 2221Substrate 1By similarity
Metal bindingi238 – 2381MagnesiumBy similarity
Active sitei253 – 2531Schiff-base intermediate with substrateBy similarity
Binding sitei279 – 2791Substrate 2By similarity
Binding sitei318 – 3181Substrate 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

Enzyme and pathway databases

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
OrganismiPropionibacterium freudenreichii subsp. freudenreichii
Taxonomic identifieri66712 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Delta-aminolevulinic acid dehydratasePRO_0000140506Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP77923.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

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.

P77923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADISIDPIV QRPRRLRRTP AIRRMVAETR LDPADLVLPM FAVEGLTEPR
60 70 80 90 100
EIATMPGVWQ HTKESLQKAV HDAADAGVGA VMLFGTPLER DPIGSQAWNP
110 120 130 140 150
HGILANAVRW AVEAEPELPV IADVCLDEFT DHGHCGVLAP DGTVDNDATL
160 170 180 190 200
PLYAKMSVVL ADAGAAMLGP SGMMDGQIAV IRKALDDAGH TDTVLMAYSA
210 220 230 240 250
KYASGFFGPF REAVDSQLKG DRRAYQQDPA NAIESLREIE LDLEQGADFV
260 270 280 290 300
MVKPAMAYLD VLAAARAISN VPVAAYVVSG EYSMIEFAAK AGALDRKRCI
310 320 330
MEALTSVKRA GASTIVTYWA TEVAIWLNEV RS
Length:332
Mass (Da):35,832
Last modified:February 1, 1997 - v1
Checksum:i09FDDC7E45D216CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51164 Genomic DNA. Translation: AAB07863.1.
D85417 Genomic DNA. Translation: BAA21911.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51164 Genomic DNA. Translation: AAB07863.1.
D85417 Genomic DNA. Translation: BAA21911.1.

3D structure databases

ProteinModelPortaliP77923.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

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. Roessner C.A.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Characterization of the hemB gene encoding delta-aminolevulinic acid dehydratase from Propionibacterium freudenreichii."
    Hashimoto Y., Yamashita Y., Ono H., Murooka Y.
    J. Ferment. Bioeng. 82:93-100(1996)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC 10470 / NRRL B-3523.

Entry informationi

Entry nameiHEM2_PROFF
AccessioniPrimary (citable) accession number: P77923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.