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P37821

- 1A1C_MALDO

UniProt

P37821 - 1A1C_MALDO

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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

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

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
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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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)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:
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 .
PIRi T16999.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 94 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