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Q43058

- HEM2_PHYPA

UniProt

Q43058 - HEM2_PHYPA

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Protein
Delta-aminolevulinic acid dehydratase, chloroplastic
Gene
HEMB, ALAD, PHYPADRAFT_221821
Organism
Physcomitrella patens subsp. patens (Moss)
Status
Reviewed - 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.

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 sitei300 – 3001Schiff-base intermediate with substrate By similarity
Binding sitei310 – 3101Substrate 1 By similarity
Binding sitei322 – 3221Substrate 1 By similarity
Metal bindingi338 – 3381Magnesium By similarity
Active sitei353 – 3531Schiff-base intermediate with substrate By similarity
Binding sitei379 – 3791Substrate 2 By similarity
Binding sitei418 – 4181Substrate 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
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 – ?Chloroplast Reviewed prediction

Interactioni

Subunit structurei

Homooctamer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ43058.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALADH family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.

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

MVGVMMAAAA TPGCGVSQAL TACGSHEGLR RVAPVFGPGV VSVSAPCKLP    50
RKLNVQAVAE PIAKSSPRTI EECEANVVAG NAPAAPPVPA KPSAPEGTPA 100
ISPLVMPARP RRNRRSPALR AAFQETTISP ANFILPLFVH EGEQNAPIGA 150
MPGCQRLGWR HGLIDEVYKA RDVGVNSVVL FPKVPDALKS STGDEAYNPD 200
GLVPRCIRLL KDKFPDLVIY TDVALDPYSS DGHDGIVRED GLIMNDETVH 250
QLCKQAVAQA QAGADVVSPS DMMDGRVGAI RKALDLAGHQ DVSIMAYTAK 300
YASAFYGPFR EALDSNPRFG DKKTYQMNPA NYREALIETR MDEAEGADIL 350
MVKPAMPYLD VIRLLRDNTA LPISAYQVSG EYSMIRAAAA AGMLDEKKAV 400
LESLLSIRRA GADVILTYFA IQAAQWLCAE RV 432
Length:432
Mass (Da):46,263
Last modified:September 3, 2014 - v2
Checksum:iE90018ADAAAA12FD
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89886 mRNA. Translation: CAA61978.1.
DS545108 Genomic DNA. Translation: EDQ57858.1.
PIRiS58169.
UniGeneiPpa.5213.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89886 mRNA. Translation: CAA61978.1 .
DS545108 Genomic DNA. Translation: EDQ57858.1 .
PIRi S58169.
UniGenei Ppa.5213.

3D structure databases

ProteinModelPortali Q43058.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0113.
HOGENOMi HOG000020323.

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

« 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: September 3, 2014
This is version 75 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

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