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Protein

1-aminocyclopropane-1-carboxylate synthase

Gene

ACS-1

Organism
Malus domestica (Apple) (Pyrus malus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 (ACS-1)
  2. 1-aminocyclopropane-1-carboxylate oxidase 1, 1-aminocyclopropane-1-carboxylate oxidase 2 (ACO2)
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

  • 1-aminocyclopropane-1-carboxylate synthase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • pyridoxal phosphate binding Source: UniProtKB

GO - Biological processi

  • ethylene biosynthetic process Source: UniProtKB
  • fruit ripening Source: UniProtKB-KW
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

BRENDAi4.4.1.14. 3165.
SABIO-RKP37821.
UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase (EC:4.4.1.14)
Short name:
ACC synthase
Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase
Gene namesi
Name:ACS-1
OrganismiMalus domestica (Apple) (Pyrus malus)
Taxonomic identifieri3750 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001239151 – 4731-aminocyclopropane-1-carboxylate synthaseAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei273N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1473
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni6 – 8Combined sources3
Helixi18 – 28Combined sources11
Beta strandi33 – 35Combined sources3
Beta strandi39 – 42Combined sources4
Helixi52 – 61Combined sources10
Helixi65 – 67Combined sources3
Helixi76 – 81Combined sources6
Helixi89 – 102Combined sources14
Turni103 – 105Combined sources3
Helixi111 – 113Combined sources3
Beta strandi114 – 118Combined sources5
Helixi119 – 131Combined sources13
Beta strandi137 – 143Combined sources7
Helixi148 – 151Combined sources4
Turni152 – 156Combined sources5
Beta strandi159 – 164Combined sources6
Helixi167 – 169Combined sources3
Helixi175 – 187Combined sources13
Beta strandi192 – 200Combined sources9
Turni202 – 204Combined sources3
Helixi210 – 223Combined sources14
Beta strandi226 – 230Combined sources5
Helixi234 – 236Combined sources3
Beta strandi239 – 241Combined sources3
Helixi246 – 249Combined sources4
Turni250 – 254Combined sources5
Beta strandi256 – 260Combined sources5
Helixi261 – 264Combined sources4
Beta strandi265 – 275Combined sources11
Helixi278 – 280Combined sources3
Beta strandi282 – 288Combined sources7
Helixi290 – 299Combined sources10
Helixi300 – 302Combined sources3
Helixi307 – 318Combined sources12
Helixi320 – 346Combined sources27
Turni347 – 349Combined sources3
Beta strandi357 – 364Combined sources8
Helixi366 – 368Combined sources3
Beta strandi369 – 373Combined sources5
Helixi374 – 386Combined sources13
Helixi395 – 398Combined sources4
Beta strandi405 – 409Combined sources5
Beta strandi411 – 413Combined sources3
Helixi415 – 432Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8GX-ray2.37A/B3-431[»]
1M4NX-ray2.01A1-435[»]
1M7YX-ray1.60A1-435[»]
1YNUX-ray2.25A1-473[»]
3PIUX-ray1.35A1-435[»]
ProteinModelPortaliP37821.
SMRiP37821.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37821.

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.

P37821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL
60 70 80 90 100
CFDLLESWLA KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA
110 120 130 140 150
EIRGNKVTFD PNHLVLTAGA TSANETFIFC LADPGEAVLI PTPYYPGFDR
160 170 180 190 200
DLKWRTGVEI VPIHCTSSNG FQITETALEE AYQEAEKRNL RVKGVLVTNP
210 220 230 240 250
SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS PSFISVMEVL
260 270 280 290 300
KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS
310 320 330 340 350
SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI
360 370 380 390 400
SCLNGNAGLF CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC
410 420 430 440 450
TEPGWFRVCF ANLPERTLDL AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS
460 470
RRQSLTKWVS RLSFDDRGPI PGR
Length:473
Mass (Da):53,251
Last modified:July 15, 1998 - v2
Checksum:i6ACA20759615E75D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15Q → E in AAA03472 (Ref. 3) Curated1
Sequence conflicti101E → K in AAA03472 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31347 mRNA. Translation: AAA73941.1.
U89156 Genomic DNA. Translation: AAB68617.1.
U03294 mRNA. Translation: AAA03472.1.
PIRiT16999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31347 mRNA. Translation: AAA73941.1.
U89156 Genomic DNA. Translation: AAB68617.1.
U03294 mRNA. Translation: AAA03472.1.
PIRiT16999.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8GX-ray2.37A/B3-431[»]
1M4NX-ray2.01A1-435[»]
1M7YX-ray1.60A1-435[»]
1YNUX-ray2.25A1-473[»]
3PIUX-ray1.35A1-435[»]
ProteinModelPortaliP37821.
SMRiP37821.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
BRENDAi4.4.1.14. 3165.
SABIO-RKP37821.

Miscellaneous databases

EvolutionaryTraceiP37821.

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...

Entry informationi

Entry namei1A1C_MALDO
AccessioniPrimary (citable) accession number: P37821
Secondary accession number(s): O04993, Q40278
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1998
Last modified: November 2, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.