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P37821 (1A1C_MALDO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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:
1-aminocyclopropane-1-carboxylate synthase

Short name=ACC synthase
EC=4.4.1.14
Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase
Gene names
Name:ACS-1
OrganismMalus domestica (Apple) (Pyrus malus)
Taxonomic identifier3750 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.

Catalytic activity

S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine.

Cofactor

Pyridoxal phosphate.

Pathway

Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4734731-aminocyclopropane-1-carboxylate synthase
PRO_0000123915

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict151Q → E in AAA03472. Ref.3
Sequence conflict1011E → K in AAA03472. Ref.3

Secondary structure

.............................................................................. 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37821 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 6ACA20759615E75D

FASTA47353,251
        10         20         30         40         50         60 
MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL CFDLLESWLA 

        70         80         90        100        110        120 
KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA EIRGNKVTFD PNHLVLTAGA 

       130        140        150        160        170        180 
TSANETFIFC LADPGEAVLI PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITETALEE 

       190        200        210        220        230        240 
AYQEAEKRNL RVKGVLVTNP SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS 

       250        260        270        280        290        300 
PSFISVMEVL KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS 

       310        320        330        340        350        360 
SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI SCLNGNAGLF 

       370        380        390        400        410        420 
CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC TEPGWFRVCF ANLPERTLDL 

       430        440        450        460        470 
AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS RRQSLTKWVS RLSFDDRGPI PGR 

« Hide

References

[1]"A full-length cDNA encoding 1-aminocyclopropane-1-carboxylate synthase from apple."
Lay-Yee M., Knighton M.L.
Plant Physiol. 107:1017-1018(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Golden Delicious.
Tissue: Fruit cortical tissue.
[2]Harada T., Sunako T., Sakuraba W., Goto S., Senda M., Akada S., Ishikawa R., Niizeki M.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Golden Delicious.
[3]"Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase and expression of its mRNA in ripening apple fruit."
Dong J.G., Kim W.T., Yip W.K., Thompson G.A., Li L., Bennett A.B., Yang S.F.
Planta 185:38-45(1991)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-473.
Strain: cv. Golden Delicious.
Tissue: Fruit.
[4]"Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene."
Capitani G., Hohenester E., Feng L., Storici P., Kirsch J.F., Jansonius J.N.
J. Mol. Biol. 294:745-756(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31347 mRNA. Translation: AAA73941.1.
U89156 Genomic DNA. Translation: AAB68617.1.
U03294 mRNA. Translation: AAA03472.1.
PIRT16999.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8GX-ray2.37A/B3-431[»]
1M4NX-ray2.01A1-435[»]
1M7YX-ray1.60A1-435[»]
1YNUX-ray2.25A1-473[»]
3PIUX-ray1.35A1-435[»]
ProteinModelPortalP37821.
SMRP37821. Positions 3-431.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP37821.
UniPathwayUPA00384; UER00562.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP37821.

Entry information

Entry name1A1C_MALDO
AccessionPrimary (citable) accession number: P37821
Secondary accession number(s): O04993, Q40278
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 92 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways