Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P24493

- HEM2_SPIOL

UniProt

P24493 - HEM2_SPIOL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 4 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

Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei301 – 3011Schiff-base intermediate with substrateBy similarity
Binding sitei311 – 3111Substrate 1By similarity
Binding sitei323 – 3231Substrate 1By similarity
Metal bindingi339 – 3391MagnesiumBy similarity
Active sitei354 – 3541Schiff-base intermediate with substrateBy similarity
Binding sitei380 – 3801Substrate 2By similarity
Binding sitei419 – 4191Substrate 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:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:HEMB
Synonyms:ALA1
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5656Chloroplast1 PublicationAdd
BLAST
Chaini57 – 433377Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013321Add
BLAST

Interactioni

Subunit structurei

Homooctamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP24493.
SMRiP24493. Positions 110-428.
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.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[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.

P24493-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASTFNIPCN AGTIKNFNNS QRNLGFSSNL GINFAKTRFS NCGDSGRIPS
60 70 80 90 100
QLVVRASERR DNLTQQKTGL SIEECEAAVV AGNAPSAPPV PPTPKAPSGT
110 120 130 140 150
PSVSPLSLGR RPRRNRTSPV FRAAFQETTL SPANVVYPLF IHEGEEDTPI
160 170 180 190 200
GAMPGCYRLG WRHGLVEEVA KARDVVVNSI VVFPKPDALK SPTGDEAYNE
210 220 230 240 250
NGLVPRTIRM LKDKFPDLII YTDVALDPYY YDGHDGIVTQ HGVIMNDETV
260 270 280 290 300
HQLCKQAVAQ ARAGADVVSP SDMMDGRVGA IRAALDAEGY SNVSIMSYTA
310 320 330 340 350
KYASSFYGPF REALDSNPRF GDKKTYQMNP ANYREALIET QEDESEGADI
360 370 380 390 400
LLVKPGLPYL DIIRLLRDNS DLPIAAYQVS GEYSMIKAGG VLKMIDEEKV
410 420 430
MLESLLCLRR AGADIILTYF ALQAARCLCG EKR
Length:433
Mass (Da):47,322
Last modified:November 1, 1995 - v2
Checksum:i4B02E3EFC4BBE131
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57842 mRNA. Translation: CAA40974.1.
PIRiA50000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57842 mRNA. Translation: CAA40974.1 .
PIRi A50000.

3D structure databases

ProteinModelPortali P24493.
SMRi P24493. Positions 110-428.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 ]
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of plastid 5-aminolevulinate dehydratase (ALAD; EC 4.2.1.24) from spinach (Spinacia oleracea L.) by sequencing and comparison with non-plant ALAD enzymes."
    Schaumburg A., Schneider-Poetsch H.A.W., Eckerskorn C.
    Z. Naturforsch. C 47:77-84(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-70.
    Strain: cv. Aestivato.

Entry informationi

Entry nameiHEM2_SPIOL
AccessioniPrimary (citable) accession number: P24493
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3