ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P24493

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HEM2_SPIOL
Primary accession number P24493
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on November 1, 1995 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Delta-aminolevulinic acid dehydratase, chloroplastic [Precursor]
Synonyms ALADH
ALAD
EC 4.2.1.24
Porphobilinogen synthase
Gene name
Name: ALA1
From
Spinacia oleracea (Spinach) [TaxID: 3562] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; Caryophyllales; Amaranthaceae; Spinacia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 57-70.
STRAIN=cv. Aestivato;
PubMed=1351729 [NCBI, ExPASy, EBI, Israel, Japan]
Schaumburg A., Schneider-Poetsch H.A.W., Eckerskorn C.;
"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.";
Z. Naturforsch. C 47:77-84(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X57842; CAA40974.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A50000; A50000.
3D structure databases
HSSP P13716; 1E51. [HSSP ENTRY / PDB]
ModBase P24493.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004655; Molecular function: porphobilinogen synthase activity (inferred from electronic annotation from InterPro).
GO:0015995; Biological process: chlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001731; 4pyrrol_synth_porphobiln_synth.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
PANTHER PTHR11458; AlaD_dehydratase; 1.
Pfam PF00490; ALAD; 1.
Pfam graphical view of domain structure.
PRINTS PR00144; DALDHYDRTASE.
ProDom PD002304; AlaD_dehydratase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00169; D_ALA_DEHYDRATASE; 1.
ProtoNet P24493.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chlorophyll biosynthesis; Chloroplast; Direct protein sequencing; Lyase; Magnesium; Plastid; Porphyrin biosynthesis; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    56  56     Chloroplast. 
CHAIN   57   433  377     Delta-aminolevulinic acid dehydratase, chloroplastic. PRO_0000013321
REGION   222   240  19     Magnesium-binding (By similarity). 
ACT_SITE   354   354        By similarity. 
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 47322 Da [This is the MW of the unprocessed precursor] CRC64: 4B02E3EFC4BBE131 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MASTFNIPCN AGTIKNFNNS QRNLGFSSNL GINFAKTRFS NCGDSGRIPS QLVVRASERR 

        70         80         90        100        110        120 
DNLTQQKTGL SIEECEAAVV AGNAPSAPPV PPTPKAPSGT PSVSPLSLGR RPRRNRTSPV 

       130        140        150        160        170        180 
FRAAFQETTL SPANVVYPLF IHEGEEDTPI GAMPGCYRLG WRHGLVEEVA KARDVVVNSI 

       190        200        210        220        230        240 
VVFPKPDALK SPTGDEAYNE NGLVPRTIRM LKDKFPDLII YTDVALDPYY YDGHDGIVTQ 

       250        260        270        280        290        300 
HGVIMNDETV HQLCKQAVAQ ARAGADVVSP SDMMDGRVGA IRAALDAEGY SNVSIMSYTA 

       310        320        330        340        350        360 
KYASSFYGPF REALDSNPRF GDKKTYQMNP ANYREALIET QEDESEGADI LLVKPGLPYL 

       370        380        390        400        410        420 
DIIRLLRDNS DLPIAAYQVS GEYSMIKAGG VLKMIDEEKV MLESLLCLRR AGADIILTYF 

       430 
ALQAARCLCG EKR
P24493 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!