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Q42682

- HEM2_CHLRE

UniProt

Q42682 - HEM2_CHLRE

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Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene
HEMB, ALAD
Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - 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.

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

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 substrate By similarity
Binding sitei261 – 2611Substrate 1 By similarity
Binding sitei281 – 2811Substrate 1 By similarity
Metal bindingi297 – 2971Magnesium By similarity
Active sitei312 – 3121Schiff-base intermediate with substrate By similarity
Binding sitei338 – 3381Substrate 2 By similarity
Binding sitei377 – 3771Substrate 2 By 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 stroma Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Chloroplast Reviewed predictionAdd
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.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALADH family.

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

MQMMQRNVVG QRPVAGSRRS LVVANVAEVT RPAVSTNGKH RTGVPEGTPI    50
VTPQDLPSRP RRNRRSESFR ASVREVNVSP ANFILPIFIH EESNQNVPIA 100
SMPGINRLAY GKNVIDYVAE PRSYGVNQVV VFPKTPDHLK TQTAEEAFNK 150
NGLSQRTIRL LKDSFPDLEV YTDVALDPYN SDGHDGIVSD AGVILNDETI 200
EYLCRQAVSQ AEAGADVVSP SDMMDGRVGA IRRALDREGF TNVSIMSYTA 250
KYASAYYGPF RDALASAPKP GQAHRRIPPN KKTYQMDPAN YREAIREAKA 300
DEAEGADIMM VKPGMPYLDV VRLLRETSPL PVAVYHVSGE YAMLKAAAER 350
GWLNEKDAVL EAMTCFRRAG GDLILTYYGI EASKWLAGEK 390
Length:390
Mass (Da):43,046
Last modified:November 1, 1997 - v1
Checksum:i6114C4E0325A4242
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19876 mRNA. Translation: AAA79515.1.
PIRiS53487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19876 mRNA. Translation: AAA79515.1 .
PIRi S53487.

3D structure databases

ProteinModelPortali Q42682.
SMRi Q42682. Positions 58-387.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q42682.
ProMEXi Q42682.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0113.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .

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. "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: March 19, 2014
This is version 72 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

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