Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q01912 (1A1C_VIGRR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-aminocyclopropane-1-carboxylate synthase

Short name=ACC synthase
EC=4.4.1.14
Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase
Gene names
Name:ACS5
OrganismVigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Taxonomic identifier3916 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Protein attributes

Sequence length368 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.

Subunit structure

Homodimer.

Induction

Hormones, such as auxin, environmental factors, such as mechanical wounding and a number of chemicals.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›368›3681-aminocyclopropane-1-carboxylate synthase
PRO_0000123917

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Non-terminal residue11
Non-terminal residue3681

Sequences

Sequence LengthMass (Da)Tools
Q01912 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 31BA61D5FC2D4CB8

FASTA36841,477
        10         20         30         40         50         60 
QMGLAENQLT SDLVEDWILN NPEASICTPE GINDFRAIAN FQDYHGLAEF RNAVAKFMAR 

        70         80         90        100        110        120 
TRGNRITFDP DRIVMSGGAT GAHEVTAFCL ADPGEAFLVP IPYYPGFDRD LRWRTGVKLV 

       130        140        150        160        170        180 
PVMCDSSNNF VLTKEALEDA YEKAREDNIR VKGLLITNPS NPLGTIMDRK TLRTVVSFIN 

       190        200        210        220        230        240 
EKRIHLVCDE IYAATVFSQP GFISIAEILE DETDIECDRN LVHIVYSLSK DMGFPGFRVG 

       250        260        270        280        290        300 
IIYSYNDAVV NCARKMSSFG LVSTQTQYLL ASMLNDDEFV ERFLAESAKR LAQRFRVFTG 

       310        320        330        340        350        360 
GLAKVGIKCL QSNAGLFVWM DLRQLLKKPT FDSETELWKV IIHEVKINVS PGYSFHCTEP 


GWFRVCFA 

« Hide

References

[1]"Identification and characterization of a full-length cDNA encoding for an auxin-induced 1-aminocyclopropane-1-carboxylate synthase from etiolated mung bean hypocotyl segments and expression of its mRNA in response to indole-3-acetic acid."
Botella J.R., Arteca J.M., Schlagnhaufer C.D., Arteca R.N., Phillips A.T.
Plant Mol. Biol. 20:425-436(1992) [PubMed: 1421146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Berken / Rwilcz.
Tissue: Hypocotyl.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11562 mRNA. Translation: CAA77655.1.

3D structure databases

ProteinModelPortalQ01912.
SMRQ01912. Positions 1-368.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00753. ACCSYNTHASE.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name1A1C_VIGRR
AccessionPrimary (citable) accession number: Q01912
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 31, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families