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Protein

Delta-aminolevulinic acid dehydratase, chloroplastic

Gene

HEMB

Organism
Physcomitrella patens subsp. patens (Moss)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei300 – 3001Schiff-base intermediate with substrateBy similarity
Binding sitei310 – 3101Substrate 1By similarity
Binding sitei322 – 3221Substrate 1By similarity
Metal bindingi338 – 3381MagnesiumBy similarity
Active sitei353 – 3531Schiff-base intermediate with substrateBy similarity
Binding sitei379 – 3791Substrate 2By similarity
Binding sitei418 – 4181Substrate 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
ORF Names:PHYPADRAFT_221821
OrganismiPhyscomitrella patens subsp. patens (Moss)
Taxonomic identifieri3218 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
ProteomesiUP000006727: Partially assembled WGS sequence

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
Chaini? – 432Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013318
Transit peptidei1 – ?ChloroplastSequence Analysis

Interactioni

Subunit structurei

Homooctamer.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.

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.

Q43058-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGVMMAAAA TPGCGVSQAL TACGSHEGLR RVAPVFGPGV VSVSAPCKLP
60 70 80 90 100
RKLNVQAVAE PIAKSSPRTI EECEANVVAG NAPAAPPVPA KPSAPEGTPA
110 120 130 140 150
ISPLVMPARP RRNRRSPALR AAFQETTISP ANFILPLFVH EGEQNAPIGA
160 170 180 190 200
MPGCQRLGWR HGLIDEVYKA RDVGVNSVVL FPKVPDALKS STGDEAYNPD
210 220 230 240 250
GLVPRCIRLL KDKFPDLVIY TDVALDPYSS DGHDGIVRED GLIMNDETVH
260 270 280 290 300
QLCKQAVAQA QAGADVVSPS DMMDGRVGAI RKALDLAGHQ DVSIMAYTAK
310 320 330 340 350
YASAFYGPFR EALDSNPRFG DKKTYQMNPA NYREALIETR MDEAEGADIL
360 370 380 390 400
MVKPAMPYLD VIRLLRDNTA LPISAYQVSG EYSMIRAAAA AGMLDEKKAV
410 420 430
LESLLSIRRA GADVILTYFA IQAAQWLCAE RV
Length:432
Mass (Da):46,263
Last modified:September 3, 2014 - v2
Checksum:iE90018ADAAAA12FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151G → R in CAA61978 (Ref. 1) Curated
Sequence conflicti24 – 241G → S in CAA61978 (Ref. 1) Curated
Sequence conflicti212 – 2143DKF → AI in CAA61978 (Ref. 1) Curated
Sequence conflicti295 – 2951M → I in CAA61978 (Ref. 1) Curated
Sequence conflicti309 – 3091F → S in CAA61978 (Ref. 1) Curated
Sequence conflicti388 – 3914AAAA → GCR in CAA61978 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89886 mRNA. Translation: CAA61978.1.
DS545108 Genomic DNA. Translation: EDQ57858.1.
PIRiS58169.
RefSeqiXP_001777328.1. XM_001777276.1.
UniGeneiPpa.5213.

Genome annotation databases

GeneIDi5940528.
KEGGippp:PHYPADRAFT_221821.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89886 mRNA. Translation: CAA61978.1.
DS545108 Genomic DNA. Translation: EDQ57858.1.
PIRiS58169.
RefSeqiXP_001777328.1. XM_001777276.1.
UniGeneiPpa.5213.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5940528.
KEGGippp:PHYPADRAFT_221821.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.

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

Publicationsi

« Hide 'large scale' publications
  1. Gwarek M.A.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants."
    Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y.
    , Hashimoto S.-I., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L.
    Science 319:64-69(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Gransden 2004.

Entry informationi

Entry nameiHEM2_PHYPA
AccessioniPrimary (citable) accession number: Q43058
Secondary accession number(s): A9TFG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 3, 2014
Last modified: February 4, 2015
This is version 80 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, Complete proteome, Reference proteome

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.