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Q9SFH9 (HEM21_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-aminolevulinic acid dehydratase 1, chloroplastic

Short name=ALADH1
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:HEMB1
Ordered Locus Names:At1g69740
ORF Names:T6C23.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

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

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Porphyrin-containing compound metabolism; chlorophyll biosynthesis.

Subunit structure

Homooctamer By similarity.

Subcellular location

Plastidchloroplast By similarity.

Tissue specificity

Highly expressed in cotyledons during dark-to-light transition. Ref.4

Induction

Up-regulated by the transcription factors FAR1 and FHY3. Ref.4

Disruption phenotype

Embryo lethal when homozygous. Impaired plant growth and development. Ref.4

Sequence similarities

Belongs to the ALADH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Chloroplast Potential
Chain53 – 430378Delta-aminolevulinic acid dehydratase 1, chloroplastic
PRO_0000013314

Regions

Compositional bias81 – 10121Pro-rich

Sites

Active site2981Schiff-base intermediate with substrate By similarity
Active site3511Schiff-base intermediate with substrate By similarity
Metal binding3361Magnesium By similarity
Binding site3081Substrate 1 By similarity
Binding site3201Substrate 1 By similarity
Binding site3771Substrate 2 By similarity
Binding site4161Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SFH9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 44B0984247FC6147

FASTA43046,690
        10         20         30         40         50         60 
MATTPIFNAS CSFPSTRGID CKSYIGLRSN VSKVSVASSR IATSQRRNLV VRASESGNGH 

        70         80         90        100        110        120 
AKKLGMSDAE CEAAVAAGNV PEAPPVPPKP AAPVGTPIIK PLNLSRRPRR NRASPVTRAA 

       130        140        150        160        170        180 
FQETDISPAN FVYPLFIHEG EEDTPIGAMP GCYRLGWRHG LVQEVAKARA VGVNSIVLFP 

       190        200        210        220        230        240 
KVPEALKNST GDEAYNDNGL VPRTIRLLKD KYPDLIIYTD VALDPYSSDG HDGIVREDGV 

       250        260        270        280        290        300 
IMNDETVHQL CKQAVSQARA GADVVSPSDM MDGRVGAIRS ALDAEGFQNV SIMSYTAKYA 

       310        320        330        340        350        360 
SSFYGPFREA LDSNPRFGDK KTYQMNPANY REALIEARED EAEGADILLV KPGLPYLDII 

       370        380        390        400        410        420 
RLLRDKSPLP IAAYQVSGEY SMIKAGGVLK MIDEEKVMME SLMCLRRAGA DIILTYFALQ 

       430 
AATCLCGEKR 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Transposase-derived proteins FHY3/FAR1 interact with PHYTOCHROME-INTERACTING FACTOR1 to regulate chlorophyll biosynthesis by modulating HEMB1 during deetiolation in Arabidopsis."
Tang W., Wang W., Chen D., Ji Q., Jing Y., Wang H., Lin R.
Plant Cell 24:1984-2000(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY FHY3 AND FAR1, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC013289 Genomic DNA. Translation: AAG52549.1.
CP002684 Genomic DNA. Translation: AEE34969.1.
CP002684 Genomic DNA. Translation: AEE34970.1.
AF327428 mRNA. Translation: AAG42018.1.
AF361803 mRNA. Translation: AAK32816.1.
AY059154 mRNA. Translation: AAL15379.1.
AY081254 mRNA. Translation: AAL91143.1.
AY113941 mRNA. Translation: AAM44989.1.
AY120705 mRNA. Translation: AAM53263.1.
AY128711 mRNA. Translation: AAM91111.1.
PIRD96719.
RefSeqNP_001077800.1. NM_001084331.2.
NP_177132.1. NM_105642.3.
UniGeneAt.10020.
At.21048.

3D structure databases

ProteinModelPortalQ9SFH9.
SMRQ9SFH9. Positions 102-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid28531. 1 interaction.
STRING3702.AT1G69740.2-P.

Proteomic databases

PaxDbQ9SFH9.
PRIDEQ9SFH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G69740.1; AT1G69740.1; AT1G69740.
AT1G69740.2; AT1G69740.2; AT1G69740.
GeneID843310.
KEGGath:AT1G69740.

Organism-specific databases

TAIRAT1G69740.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
InParanoidQ9SFH9.
KOK01698.
OMAGEYAMVE.
PhylomeDBQ9SFH9.
ProtClustDBCLSN2679842.

Enzyme and pathway databases

BioCycARA:GQT-2417-MONOMER.
UniPathwayUPA00251; UER00318.
UPA00668.

Gene expression databases

GenevestigatorQ9SFH9.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9SFH9.

Entry information

Entry nameHEM21_ARATH
AccessionPrimary (citable) accession number: Q9SFH9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names