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Protein

1-aminocyclopropane-1-carboxylate synthase CMA101

Gene

ACS2

Organism
Cucurbita maxima (Pumpkin) (Winter squash)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Pathwayi: ethylene biosynthesis via S-adenosyl-L-methionine

This protein is involved in step 1 of the subpathway that synthesizes ethylene from S-adenosyl-L-methionine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 1-aminocyclopropane-1-carboxylate synthase CMA101 (ACS2), 1-aminocyclopropane-1-carboxylate synthase CMW33 (ACS1)
  2. no protein annotated in this organism
This subpathway is part of the pathway ethylene biosynthesis via S-adenosyl-L-methionine, which is itself part of Alkene biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ethylene from S-adenosyl-L-methionine, the pathway ethylene biosynthesis via S-adenosyl-L-methionine and in Alkene biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Ethylene biosynthesis, Fruit ripening

Keywords - Ligandi

Pyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase CMA101 (EC:4.4.1.14)
Short name:
ACC synthase
Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase
Gene namesi
Name:ACS2
Synonyms:PCVV4A
OrganismiCucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifieri3661 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4754751-aminocyclopropane-1-carboxylate synthase CMA101PRO_0000123908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysineBy similarity

Expressioni

Inductioni

By tissue wounding and auxin.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliQ00257.
SMRiQ00257. Positions 12-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00257-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMLSTKATC NSHGQDSSYF LGWEAYENNP FHHTSNPNGI IQMGLAENQL
60 70 80 90 100
SFDLLESWLS KNPDAASFKR DGKSIFRELA LFQDYHGLPA FKKALVEFMA
110 120 130 140 150
EIRGNKVSFE ANNIVLTAGA TSANETLMFC LAEAGDAFLL PTPYYPGFDR
160 170 180 190 200
DLKWRTGVEI VPIHCTSSNG FQITQSALEQ AYKDAQTRNL RVKGVLVTNP
210 220 230 240 250
SNPLGTTMNR DELNLVFDFI TSKGIHLISD EIYSGTVFGS PGFVSAMEVL
260 270 280 290 300
KERSSEDEEV WKRVHIVYSL SKDLGLPGFR VGAIYSNDDM VVAAATKMSS
310 320 330 340 350
FGLVSSQTQY LLSAMLSDKK FTISYISENQ KRLKQRQKML VSGLQKAGIN
360 370 380 390 400
CLDSNAGLFC WVDMRHLLES DKFESELELW KKIVYEVGLN ISPGSSCHCT
410 420 430 440 450
EPGWFRVCFA NMSESTLKLA VRRLKSFVTE LRSTTTSNHR NHDNKICKNI
460 470
KKNIFTKWVF RQSAQEANRK MQAER
Length:475
Mass (Da):53,481
Last modified:July 1, 1993 - v1
Checksum:iD02A666E137F44A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37774 Genomic DNA. Translation: AAA91152.1.
D01033 mRNA. Translation: BAA00839.1.
PIRiJQ2214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37774 Genomic DNA. Translation: AAA91152.1.
D01033 mRNA. Translation: BAA00839.1.
PIRiJQ2214.

3D structure databases

ProteinModelPortaliQ00257.
SMRiQ00257. Positions 12-430.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry namei1A12_CUCMA
AccessioniPrimary (citable) accession number: Q00257
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 6, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.