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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: 5 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 (PubMed:7809054, PubMed:11591146). Catalyzes also the conversion of L-vinylglycine (L-VG) to alpha-ketobutyrate and ammonia (PubMed:10704193). Can use S-methylmethionine as substrate (PubMed:14678788).4 Publications

Catalytic activityi

S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine.2 Publications
2-aminobut-3-enoate = 2-oxobutanoate + ammonia.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Enzyme regulationi

Inhibited by L-aminoethoxyvinylglycine (AVG) (PubMed:12228256). Inhibited by L-vinylglycine (L-VG) (PubMed:10704193). Inhibited by S-methylmethionine through a L-VG ketimine intermediate (PubMed:14678788).3 Publications

Kineticsi

kcat is 9 sec(-1) per monomer with S-adenosyl-L-methionine as substrate (PubMed:7809054). kcat is 1.8 sec(-1) with L-vinylglycine as substrate (PubMed:10704193). kcat is 2.7 min(-1) with S-methylmethionine as substrate (PubMed:14678788).3 Publications
  1. KM=12 µM for S-adenosyl-L-methionine1 Publication
  2. KM=1.4 mM for L-vinylglycine1 Publication
  3. KM=4 mM for S-methylmethionine1 Publication

    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.Curated
    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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei145SubstrateCombined sources1 Publication1
    Binding sitei151SubstrateCombined sources1 Publication1

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywordsi

    Molecular functionLyase, Oxidoreductase
    Biological processEthylene biosynthesis, Fruit ripening
    LigandPyridoxal phosphate, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi4.4.1.14. 3165.
    SABIO-RKiP37821.
    UniPathwayiUPA00384; UER00562.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-aminocyclopropane-1-carboxylate synthase1 Publication (EC:1.4.-.-1 Publication, EC:4.4.1.142 Publications)
    Short name:
    ACC synthase
    Alternative name(s):
    S-adenosyl-L-methionine methylthioadenosine-lyase
    Gene namesi
    Name:ACS-11 Publication
    OrganismiMalus domestica (Apple) (Pyrus malus)
    Taxonomic identifieri3750 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi46A → V: Reduced activity. 1 Publication1
    Mutagenesisi47E → D or Q: Decreased catalytic activity and reaction specificity. 1 Publication1
    Mutagenesisi85Y → A: Strongly reduced catalytic activity. 1 Publication1
    Mutagenesisi230D → N: Loss of catalytic activity. 1 Publication1
    Mutagenesisi233Y → A: Decreased affinity for the substrate. 1 Publication1
    Mutagenesisi273K → A: Loss of catalytic activity. 2 Publications1
    Mutagenesisi407R → K: Strongly decreased catalytic activity. 1 Publication1

    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)lysineCombined sources2 Publications1

    Expressioni

    Developmental stagei

    Expressed during ripening.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni84 – 85Substrate bindingCombined sources1 Publication2

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    InterProiView protein in InterPro
    IPR004839. Aminotransferase_I/II.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_sub2.
    PfamiView protein in Pfam
    PF00155. Aminotran_1_2. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiView protein in PROSITE
    PS00105. AA_TRANSFER_CLASS_1. 1 hit.

    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 (PubMed:24186277).Curated1
    Sequence conflicti101E → K in AAA03472 (PubMed:24186277).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.

    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.

    Entry informationi

    Entry namei1A1C_MALDO
    AccessioniPrimary (citable) accession number: P37821
    Secondary accession number(s): O04993, Q40278
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 15, 1998
    Last modified: April 12, 2017
    This is version 103 of the entry and version 2 of the sequence. See 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