Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P37821

- 1A1C_MALDO

UniProt

P37821 - 1A1C_MALDO

Protein

1-aminocyclopropane-1-carboxylate synthase

Gene

ACS-1

Organism
Malus domestica (Apple) (Pyrus malus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. 1-aminocyclopropane-1-carboxylate synthase activity Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB
    3. pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    1. 1-aminocyclopropane-1-carboxylate biosynthetic process Source: GOC
    2. ethylene biosynthetic process Source: UniProtKB
    3. fruit ripening Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Ethylene biosynthesis, Fruit ripening

    Keywords - Ligandi

    Pyridoxal phosphate, S-adenosyl-L-methionine

    Enzyme and pathway databases

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4734731-aminocyclopropane-1-carboxylate synthasePRO_0000123915Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei273 – 2731N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    473
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni6 – 83
    Helixi18 – 2811
    Beta strandi33 – 353
    Beta strandi39 – 424
    Helixi52 – 6110
    Helixi65 – 673
    Helixi76 – 816
    Helixi89 – 10214
    Turni103 – 1053
    Helixi111 – 1133
    Beta strandi114 – 1185
    Helixi119 – 13113
    Beta strandi137 – 1437
    Helixi148 – 1514
    Turni152 – 1565
    Beta strandi159 – 1646
    Helixi167 – 1693
    Helixi175 – 18713
    Beta strandi192 – 2009
    Turni202 – 2043
    Helixi210 – 22314
    Beta strandi226 – 2305
    Helixi234 – 2363
    Beta strandi239 – 2413
    Helixi246 – 2494
    Turni250 – 2545
    Beta strandi256 – 2605
    Helixi261 – 2644
    Beta strandi265 – 27511
    Helixi278 – 2803
    Beta strandi282 – 2887
    Helixi290 – 29910
    Helixi300 – 3023
    Helixi307 – 31812
    Helixi320 – 34627
    Turni347 – 3493
    Beta strandi357 – 3648
    Helixi366 – 3683
    Beta strandi369 – 3735
    Helixi374 – 38613
    Helixi395 – 3984
    Beta strandi405 – 4095
    Beta strandi411 – 4133
    Helixi415 – 43218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 3-431.
    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

    MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL    50
    CFDLLESWLA KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA 100
    EIRGNKVTFD PNHLVLTAGA TSANETFIFC LADPGEAVLI PTPYYPGFDR 150
    DLKWRTGVEI VPIHCTSSNG FQITETALEE AYQEAEKRNL RVKGVLVTNP 200
    SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS PSFISVMEVL 250
    KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS 300
    SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI 350
    SCLNGNAGLF CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC 400
    TEPGWFRVCF ANLPERTLDL AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS 450
    RRQSLTKWVS RLSFDDRGPI PGR 473
    Length:473
    Mass (Da):53,251
    Last modified:July 15, 1998 - v2
    Checksum:i6ACA20759615E75D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151Q → E in AAA03472. 1 PublicationCurated
    Sequence conflicti101 – 1011E → K in AAA03472. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L31347 mRNA. Translation: AAA73941.1 .
    U89156 Genomic DNA. Translation: AAB68617.1 .
    U03294 mRNA. Translation: AAA03472.1 .
    PIRi T16999.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B8G X-ray 2.37 A/B 3-431 [» ]
    1M4N X-ray 2.01 A 1-435 [» ]
    1M7Y X-ray 1.60 A 1-435 [» ]
    1YNU X-ray 2.25 A 1-473 [» ]
    3PIU X-ray 1.35 A 1-435 [» ]
    ProteinModelPortali P37821.
    SMRi P37821. Positions 3-431.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00384 ; UER00562 .
    SABIO-RK P37821.

    Miscellaneous databases

    EvolutionaryTracei P37821.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004839. 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 ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).

    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: October 1, 2014
    This is version 93 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

    External Data

    Dasty 3