Reviewed, UniProtKB/Swiss-Prot P23279 (1A11_CUCPE)

Names and origin

Protein names

Recommended name:
    1-aminocyclopropane-1-carboxylate synthase 1
      Short name=ACC synthase 1
    EC=4.4.1.14
Alternative name(s):
    S-adenosyl-L-methionine methylthioadenosine-lyase

Gene names

Name:

ACC1A

Organism

Cucurbita pepo (Vegetable marrow) (Summer squash)

Taxonomic identifier

3663 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Cucurbita

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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	By wounding in fruit and etiolated hypocotyls. By indoleacetic acid (IAA)/benzyladenine/LiCl only in fruit tissue.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Ethylene biosynthesis Fruit ripening
Ligand	Pyridoxal phosphate S-adenosyl-L-methionine
Molecular function	Lyase
Gene Ontology (GO)
Biological process	ethylene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 493	493	1-aminocyclopropane-1-carboxylate synthase 1		PRO_0000123909
Amino acid modifications
	Modified residue	279	1	N6-(pyridoxal phosphate)lysine
Experimental info
	Sequence conflict	177	1	G → R in AAA33111. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P23279-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 921DC3DFB17A8769	FASTA	493	55,780
	10 20 30 40 50 60 MGFHQIDERN QALLSKIALD DGHGENSPYF DGWKAYDNDP FHPENNPLGV IQMGLAENQL 70 80 90 100 110 120 SFDMIVDWIR KHPEASICTP EGLERFKSIA NFQDYHGLPE FRNAIANFMG KVRGGRVKFD 130 140 150 160 170 180 PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAGFDR DLKWRTRAQI IRVHCNGSNN 190 200 210 220 230 240 FQVTKAALEI AYKKAQEANM KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD 250 260 270 280 290 300 EIYSATVFKA PTFTSIAEIV EQMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR 310 320 330 340 350 360 RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRV GERHARFTKE LDKMGITCLN 370 380 390 400 410 420 SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD 430 440 450 460 470 480 DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRHRDNKLR LSFSFSGRRY DEGNVLNSPH 490 TMSPHSPLVI AKN

References

[1]	"The 1-aminocyclopropane-1-carboxylate synthase of Cucurbita. Purification, properties, expression in Escherichia coli, and primary structure determination by DNA sequence analysis." Sato T., Oeller P.W., Theologis A. J. Biol. Chem. 266:3752-3759(1991) [PubMed: 1995630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Two genes encoding 1-aminocyclopropane-1-carboxylate synthase in zucchini (Cucurbita pepo) are clustered and similar but differentially regulated." Huang P.-L., Parks J.E., Rottman W.H., Theologis A. Proc. Natl. Acad. Sci. U.S.A. 88:7021-7025(1991) [PubMed: 1871117] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M58323 mRNA. Translation: AAA33113.1. M61195 Genomic DNA. Translation: AAA33111.1.
PIR	A41141.
3D structure databases
HSSP	HSSP built from PDB template 1IAX based on UniProtKB P18485.
SMR	P23279. Positions 18-435.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.4.1.14. 1943.
Family and domain databases
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

1A11_CUCPE

Accession

Primary (citable) accession number: P23279

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	September 22, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)