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Q7M523

- 1A1D_CYBSA

UniProt

Q7M523 - 1A1D_CYBSA

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Protein

1-aminocyclopropane-1-carboxylate deaminase

Gene
N/A
Organism
Cyberlindnera saturnus (Yeast) (Williopsis saturnus)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei78 – 781Nucleophile

GO - Molecular functioni

  1. 1-aminocyclopropane-1-carboxylate deaminase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. amine catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate deaminase (EC:3.5.99.7)
Short name:
ACC deaminase
Short name:
ACCD
OrganismiCyberlindnera saturnus (Yeast) (Williopsis saturnus)
Taxonomic identifieri907340 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeCyberlindnera

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3413411-aminocyclopropane-1-carboxylate deaminasePRO_0000184512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylserine1 Publication
Modified residuei51 – 511N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 43
Beta strandi12 – 154
Beta strandi18 – 203
Helixi22 – 276
Turni28 – 303
Beta strandi32 – 387
Helixi39 – 413
Helixi50 – 556
Turni56 – 583
Helixi59 – 646
Beta strandi68 – 758
Helixi79 – 9113
Beta strandi94 – 1007
Helixi107 – 1093
Turni110 – 1156
Helixi117 – 1248
Beta strandi128 – 1314
Helixi142 – 15312
Beta strandi158 – 1614
Helixi163 – 1653
Turni169 – 1735
Helixi174 – 18916
Beta strandi194 – 20310
Helixi204 – 21310
Helixi214 – 2163
Helixi219 – 2213
Beta strandi222 – 2265
Helixi231 – 24919
Helixi274 – 28714
Turni293 – 2953
Helixi296 – 30813
Beta strandi317 – 3226
Helixi326 – 33510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ7M523.
SMRiQ7M523. Positions 1-341.

Miscellaneous databases

EvolutionaryTraceiQ7M523.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01274. ACC_deam. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7M523-1 [UniParc]FASTAAdd to Basket

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SGVAKFAKYP LTFGPSPISN LNRLSQHLGS KVNVYAKRED CNSGLAFGGN    50
KLRKLEYIVP DIVEGDYTHL VSIGGRQSNQ TRMVAALAAK LGKKCVLIQE 100
DWVPIPEAEK DVYNRVGNIE LSRIMGADVR VIEDGFDIGM RKSFANALQE 150
LEDAGHKPYP IPAGCSEHKY GGLGFVGFAD EVINQEVELG IKFDKIVVCC 200
VTGSTTAGIL AGMAQYGRQD DVIAIDASFT SEKTKEQTLR IANNTAKLIG 250
VEHEFKDFTL DTRFAYPCYG VPNEGTIEAI RTCAEQEGVL TDPVYEGKSM 300
QGLIALIKED YFKPGANVLY VHLGGAPALS AYSSFFPTKT A 341
Length:341
Mass (Da):37,061
Last modified:December 15, 2003 - v1
Checksum:i64904CDD7AA2C5FA
GO

Sequence databases

PIRiPW0041.

Cross-referencesi

Sequence databases

PIRi PW0041.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F2D X-ray 2.00 A/B/C/D 2-341 [» ]
1J0C X-ray 2.75 A/B/C/D 1-341 [» ]
1J0D X-ray 2.20 A/B/C/D 1-341 [» ]
1J0E X-ray 2.45 A/B/C/D 1-341 [» ]
ProteinModelPortali Q7M523.
SMRi Q7M523. Positions 1-341.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q7M523.

Family and domain databases

InterProi IPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
PIRSFi PIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR01274. ACC_deam. 1 hit.
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry namei1A1D_CYBSA
AccessioniPrimary (citable) accession number: Q7M523
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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