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Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator.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, chloroplastic (HEMB)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Uroporphyrinogen decarboxylase (DCUP)
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 sitei294 – 2941Schiff-base intermediate with substrateBy similarity
Binding sitei304 – 3041Substrate 1By similarity
Binding sitei316 – 3161Substrate 1By similarity
Metal bindingi332 – 3321MagnesiumBy similarity
Active sitei347 – 3471Schiff-base intermediate with substrateBy similarity
Binding sitei373 – 3731Substrate 2By similarity
Binding sitei412 – 4121Substrate 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Chlorophyll biosynthesis, 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, chloroplastic (EC:4.2.1.24)
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:HEMB
Synonyms:ALAD
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Organism-specific databases

GrameneiQ42836.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 428Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013316
Transit peptidei1 – ?ChloroplastSequence Analysis

Proteomic databases

PRIDEiQ42836.

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

STRINGi4513.MLOC_74261.2.

Structurei

3D structure databases

ProteinModelPortaliQ42836.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Keywords - Domaini

Transit peptide

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]
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q42836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTVPFSPA KVQMFQATNC HGHAGFGSSF AVPRTGPRPR SVAVRVSSEQ
60 70 80 90 100
EAAATVRAPS GRSIEECEAD AVAGRFPAPS CVCQTPKAPD GTPEIRPLDM
110 120 130 140 150
AKRPRRNRRS PALRAAFQET SISPANLVLP LFIHEGEEDA PIGAMPGCFR
160 170 180 190 200
LGWQHGLLAE VYKARDVGVN SFVLFPKVPD ALKSPTGVEA YNDNGLVPRT
210 220 230 240 250
IRLLKDKFPD IIVYTDVALD PYSSDGHDGI VRKDGVILND ETVYQLCKQA
260 270 280 290 300
VSQARAGADV VSPSNMMDGR VGAIRSALDA EGFNDVSIMS YTAKYASSFY
310 320 330 340 350
GPFREALDSN PRFGDKKTYQ MNPANYREAL LETAADEAEG ADILLVKPGL
360 370 380 390 400
PYLDIIRLSR DNSALPIAAY QVSGEYSMIK AGGALNMIDE EKVMMESLMC
410 420
LRRAGADVIL TYFARQPPAV LCGMGTAK
Length:428
Mass (Da):46,213
Last modified:November 1, 1996 - v1
Checksum:i2E3F6C37109816F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92402 mRNA. Translation: CAA63139.1.
PIRiT04472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92402 mRNA. Translation: CAA63139.1.
PIRiT04472.

3D structure databases

ProteinModelPortaliQ42836.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4513.MLOC_74261.2.

Proteomic databases

PRIDEiQ42836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiQ42836.

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]
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Bougri O.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Bonus.

Entry informationi

Entry nameiHEM2_HORVU
AccessioniPrimary (citable) accession number: Q42836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

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.