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Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei251 – 2511Schiff-base intermediate with substrateBy similarity
Binding sitei261 – 2611Substrate 1By similarity
Binding sitei281 – 2811Substrate 1By similarity
Metal bindingi297 – 2971MagnesiumBy similarity
Active sitei312 – 3121Schiff-base intermediate with substrateBy similarity
Binding sitei338 – 3381Substrate 2By similarity
Binding sitei377 – 3771Substrate 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. porphobilinogen synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-KW
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
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
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424ChloroplastSequence AnalysisAdd
BLAST
Chaini25 – 390366Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013315Add
BLAST

Proteomic databases

PRIDEiQ42682.
ProMEXiQ42682.

Interactioni

Subunit structurei

Homooctamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ42682.
SMRiQ42682. Positions 58-387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0113.

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.

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

Q42682-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQMMQRNVVG QRPVAGSRRS LVVANVAEVT RPAVSTNGKH RTGVPEGTPI
60 70 80 90 100
VTPQDLPSRP RRNRRSESFR ASVREVNVSP ANFILPIFIH EESNQNVPIA
110 120 130 140 150
SMPGINRLAY GKNVIDYVAE PRSYGVNQVV VFPKTPDHLK TQTAEEAFNK
160 170 180 190 200
NGLSQRTIRL LKDSFPDLEV YTDVALDPYN SDGHDGIVSD AGVILNDETI
210 220 230 240 250
EYLCRQAVSQ AEAGADVVSP SDMMDGRVGA IRRALDREGF TNVSIMSYTA
260 270 280 290 300
KYASAYYGPF RDALASAPKP GQAHRRIPPN KKTYQMDPAN YREAIREAKA
310 320 330 340 350
DEAEGADIMM VKPGMPYLDV VRLLRETSPL PVAVYHVSGE YAMLKAAAER
360 370 380 390
GWLNEKDAVL EAMTCFRRAG GDLILTYYGI EASKWLAGEK
Length:390
Mass (Da):43,046
Last modified:November 1, 1997 - v1
Checksum:i6114C4E0325A4242
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19876 mRNA. Translation: AAA79515.1.
PIRiS53487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19876 mRNA. Translation: AAA79515.1.
PIRiS53487.

3D structure databases

ProteinModelPortaliQ42682.
SMRiQ42682. Positions 58-387.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ42682.
ProMEXiQ42682.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0113.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

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]
ProtoNetiSearch...

Publicationsi

  1. "Structure and expression of the Chlamydomonas reinhardtii alad gene encoding the chlorophyll biosynthetic enzyme, delta-aminolevulinic acid dehydratase (porphobilinogen synthase)."
    Matters G.L., Beale S.I.
    Plant Mol. Biol. 27:607-617(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NO-.

Entry informationi

Entry nameiHEM2_CHLRE
AccessioniPrimary (citable) accession number: Q42682
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 76 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.