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Reviewed, UniProtKB/Swiss-Prot Q00257 (1A12_CUCMA)

Last modified February 9, 2010. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    1-aminocyclopropane-1-carboxylate synthase CMA101
      Short name=ACC synthase
    EC=4.4.1.14
Alternative name(s):
    S-adenosyl-L-methionine methylthioadenosine-lyase
Gene names
Name: ACS2
Synonyms: PCVV4A
OrganismCucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifier3661 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsCucurbitalesCucurbitaceaeCucurbita

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Induction

By tissue wounding and auxin.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4754751-aminocyclopropane-1-carboxylate synthase CMA101
PRO_0000123908

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q00257-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D02A666E137F44A0

FASTA47553,481
        10         20         30         40         50         60 
MKMLSTKATC NSHGQDSSYF LGWEAYENNP FHHTSNPNGI IQMGLAENQL SFDLLESWLS 

        70         80         90        100        110        120 
KNPDAASFKR DGKSIFRELA LFQDYHGLPA FKKALVEFMA EIRGNKVSFE ANNIVLTAGA 

       130        140        150        160        170        180 
TSANETLMFC LAEAGDAFLL PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITQSALEQ 

       190        200        210        220        230        240 
AYKDAQTRNL RVKGVLVTNP SNPLGTTMNR DELNLVFDFI TSKGIHLISD EIYSGTVFGS 

       250        260        270        280        290        300 
PGFVSAMEVL KERSSEDEEV WKRVHIVYSL SKDLGLPGFR VGAIYSNDDM VVAAATKMSS 

       310        320        330        340        350        360 
FGLVSSQTQY LLSAMLSDKK FTISYISENQ KRLKQRQKML VSGLQKAGIN CLDSNAGLFC 

       370        380        390        400        410        420 
WVDMRHLLES DKFESELELW KKIVYEVGLN ISPGSSCHCT EPGWFRVCFA NMSESTLKLA 

       430        440        450        460        470 
VRRLKSFVTE LRSTTTSNHR NHDNKICKNI KKNIFTKWVF RQSAQEANRK MQAER 

« Hide

References

[1]"Cloning of a complementary DNA for auxin-induced 1-aminocyclopropane-1-carboxylate synthase and differential expression of the gene by auxin and wounding."
Nakagawa N., Mori H., Yamazaki K., Imaseki H.
Plant Cell Physiol. 32:1153-1163(1991)
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Nucleotide sequence of an auxin-regulated 1-aminocyclopropane-1-carboxylic acid synthase gene from Cucurbita maxima Duch."
Nakagawa N., Kamiya Y., Imaseki H.
Plant Gene Register PGR95-110
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37774 Genomic DNA. Translation: AAA91152.1.
D01033 mRNA. Translation: BAA00839.1.
PIRJQ2214.

3D structure databases

SMRQ00257. Positions 12-430.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.4.1.14. 2176.

Family and domain databases

InterProIPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00753. ACCSYNTHASE.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name1A12_CUCMA
AccessionPrimary (citable) accession number: Q00257
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents