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Q7M523 (1A1D_CYBSA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 51. 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 deaminase

Short name=ACC deaminase
Short name=ACCD
EC=3.5.99.7
OrganismCyberlindnera saturnus (Yeast) (Williopsis saturnus)
Taxonomic identifier907340 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeCyberlindnera

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate.

Catalytic activity

1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the ACC deaminase/D-cysteine desulfhydrase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processamine catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_function1-aminocyclopropane-1-carboxylate deaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3413411-aminocyclopropane-1-carboxylate deaminase
PRO_0000184512

Sites

Active site781Nucleophile

Amino acid modifications

Modified residue11N-acetylserine Ref.1
Modified residue511N6-(pyridoxal phosphate)lysine

Secondary structure

......................................................... 341
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7M523 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 64904CDD7AA2C5FA

FASTA34137,061
        10         20         30         40         50         60 
SGVAKFAKYP LTFGPSPISN LNRLSQHLGS KVNVYAKRED CNSGLAFGGN KLRKLEYIVP 

        70         80         90        100        110        120 
DIVEGDYTHL VSIGGRQSNQ TRMVAALAAK LGKKCVLIQE DWVPIPEAEK DVYNRVGNIE 

       130        140        150        160        170        180 
LSRIMGADVR VIEDGFDIGM RKSFANALQE LEDAGHKPYP IPAGCSEHKY GGLGFVGFAD 

       190        200        210        220        230        240 
EVINQEVELG IKFDKIVVCC VTGSTTAGIL AGMAQYGRQD DVIAIDASFT SEKTKEQTLR 

       250        260        270        280        290        300 
IANNTAKLIG VEHEFKDFTL DTRFAYPCYG VPNEGTIEAI RTCAEQEGVL TDPVYEGKSM 

       310        320        330        340 
QGLIALIKED YFKPGANVLY VHLGGAPALS AYSSFFPTKT A 

« Hide

References

[1]"Properties, sequence, and synthesis in Escherichia coli of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus."
Minami R., Uchiyama K., Murakami T., Kawai J., Mikami K., Yamada T., Yokoi D., Ito H., Matsui H., Honma M.
J. Biochem. 123:1112-1118(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, CHARACTERIZATION, ACETYLATION AT SER-1.
[2]"Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus."
Yao M., Ose T., Sugimoto H., Horiuchi A., Nakagawa A., Wakatsuki S., Yokoi D., Murakami T., Honma M., Tanaka I.
J. Biol. Chem. 275:34557-34565(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[3]"Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction."
Ose T., Fujino A., Yao M., Watanabe N., Honma M., Tanaka I.
J. Biol. Chem. 278:41069-41076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

Cross-references

Sequence databases

PIRPW0041.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2DX-ray2.00A/B/C/D2-341[»]
1J0CX-ray2.75A/B/C/D1-341[»]
1J0DX-ray2.20A/B/C/D1-341[»]
1J0EX-ray2.45A/B/C/D1-341[»]
ProteinModelPortalQ7M523.
SMRQ7M523. Positions 1-341.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
PIRSFPIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR01274. ACC_deam. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ7M523.

Entry information

Entry name1A1D_CYBSA
AccessionPrimary (citable) accession number: Q7M523
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references