Skip Header

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

Delta-aminolevulinic acid dehydratase 1, chloroplastic

Gene

HEMB1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 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

Pathway:iprotoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Probable delta-aminolevulinic acid dehydratase 2, chloroplastic (HEMB2), Delta-aminolevulinic acid dehydratase 1, chloroplastic (HEMB1)
  2. Porphobilinogen deaminase, chloroplastic (HEMC)
  3. Uroporphyrinogen-III synthase, chloroplastic (UROS)
  4. Uroporphyrinogen decarboxylase 2, chloroplastic (HEME2), Uroporphyrinogen decarboxylase (At2g40490), Uroporphyrinogen decarboxylase 1, chloroplastic (HEME1)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Pathway:ichlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei298 – 2981Schiff-base intermediate with substrateBy similarity
Binding sitei308 – 3081Substrate 1By similarity
Binding sitei320 – 3201Substrate 1By similarity
Metal bindingi336 – 3361MagnesiumBy similarity
Active sitei351 – 3511Schiff-base intermediate with substrateBy similarity
Binding sitei377 – 3771Substrate 2By similarity
Binding sitei416 – 4161Substrate 2By similarity

GO - Molecular functioni

GO - Biological processi

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

BioCyciARA:GQT-2417-MONOMER.
ReactomeiREACT_340934. Heme biosynthesis.
UniPathwayiUPA00251; UER00318.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase 1, chloroplastic (EC:4.2.1.24)
Short name:
ALADH1
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:HEMB1
Ordered Locus Names:At1g69740
ORF Names:T6C23.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G69740.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Embryo lethal when homozygous. Impaired plant growth and development.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252ChloroplastSequence AnalysisAdd
BLAST
Chaini53 – 430378Delta-aminolevulinic acid dehydratase 1, chloroplasticPRO_0000013314Add
BLAST

Proteomic databases

PaxDbiQ9SFH9.
PRIDEiQ9SFH9.

Expressioni

Tissue specificityi

Highly expressed in cotyledons during dark-to-light transition.1 Publication

Inductioni

Up-regulated by the transcription factors FAR1 and FHY3.1 Publication

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

BioGridi28531. 1 interaction.
STRINGi3702.AT1G69740.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SFH9.
SMRiQ9SFH9. Positions 102-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 10121Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the ALAD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiQ9SFH9.
KOiK01698.
OMAiSTYQMDP.
PhylomeDBiQ9SFH9.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[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.

Q9SFH9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTPIFNAS CSFPSTRGID CKSYIGLRSN VSKVSVASSR IATSQRRNLV
60 70 80 90 100
VRASESGNGH AKKLGMSDAE CEAAVAAGNV PEAPPVPPKP AAPVGTPIIK
110 120 130 140 150
PLNLSRRPRR NRASPVTRAA FQETDISPAN FVYPLFIHEG EEDTPIGAMP
160 170 180 190 200
GCYRLGWRHG LVQEVAKARA VGVNSIVLFP KVPEALKNST GDEAYNDNGL
210 220 230 240 250
VPRTIRLLKD KYPDLIIYTD VALDPYSSDG HDGIVREDGV IMNDETVHQL
260 270 280 290 300
CKQAVSQARA GADVVSPSDM MDGRVGAIRS ALDAEGFQNV SIMSYTAKYA
310 320 330 340 350
SSFYGPFREA LDSNPRFGDK KTYQMNPANY REALIEARED EAEGADILLV
360 370 380 390 400
KPGLPYLDII RLLRDKSPLP IAAYQVSGEY SMIKAGGVLK MIDEEKVMME
410 420 430
SLMCLRRAGA DIILTYFALQ AATCLCGEKR
Length:430
Mass (Da):46,690
Last modified:May 1, 2000 - v1
Checksum:i44B0984247FC6147
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD96719.
RefSeqiNP_001077800.1. NM_001084331.2.
NP_177132.1. NM_105642.3.
UniGeneiAt.10020.
At.21048.

Genome annotation databases

EnsemblPlantsiAT1G69740.1; AT1G69740.1; AT1G69740.
AT1G69740.2; AT1G69740.2; AT1G69740.
GeneIDi843310.
KEGGiath:AT1G69740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD96719.
RefSeqiNP_001077800.1. NM_001084331.2.
NP_177132.1. NM_105642.3.
UniGeneiAt.10020.
At.21048.

3D structure databases

ProteinModelPortaliQ9SFH9.
SMRiQ9SFH9. Positions 102-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi28531. 1 interaction.
STRINGi3702.AT1G69740.1.

Proteomic databases

PaxDbiQ9SFH9.
PRIDEiQ9SFH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G69740.1; AT1G69740.1; AT1G69740.
AT1G69740.2; AT1G69740.2; AT1G69740.
GeneIDi843310.
KEGGiath:AT1G69740.

Organism-specific databases

TAIRiAT1G69740.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
InParanoidiQ9SFH9.
KOiK01698.
OMAiSTYQMDP.
PhylomeDBiQ9SFH9.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
UPA00668.
BioCyciARA:GQT-2417-MONOMER.
ReactomeiREACT_340934. Heme biosynthesis.

Miscellaneous databases

PROiQ9SFH9.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[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. "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.
    , 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.
    , 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.

Entry informationi

Entry nameiHEM21_ARATH
AccessioniPrimary (citable) accession number: Q9SFH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 115 of the entry and version 1 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. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.