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Protein

1-aminocyclopropane-1-carboxylate deaminase

Gene
N/A
Organism
Cyberlindnera saturnus (Yeast) (Williopsis saturnus)
Status
Reviewed-Annotation score: 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei78Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi3.5.99.7. 2588.

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001845121 – 3411-aminocyclopropane-1-carboxylate deaminaseAdd BLAST341

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylserine1 Publication1
Modified residuei51N6-(pyridoxal phosphate)lysine1

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1341
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2 – 4Combined sources3
Beta strandi12 – 15Combined sources4
Beta strandi18 – 20Combined sources3
Helixi22 – 27Combined sources6
Turni28 – 30Combined sources3
Beta strandi32 – 38Combined sources7
Helixi39 – 41Combined sources3
Helixi50 – 55Combined sources6
Turni56 – 58Combined sources3
Helixi59 – 64Combined sources6
Beta strandi68 – 75Combined sources8
Helixi79 – 91Combined sources13
Beta strandi94 – 100Combined sources7
Helixi107 – 109Combined sources3
Turni110 – 115Combined sources6
Helixi117 – 124Combined sources8
Beta strandi128 – 131Combined sources4
Helixi142 – 153Combined sources12
Beta strandi158 – 161Combined sources4
Helixi163 – 165Combined sources3
Turni169 – 173Combined sources5
Helixi174 – 189Combined sources16
Beta strandi194 – 203Combined sources10
Helixi204 – 213Combined sources10
Helixi214 – 216Combined sources3
Helixi219 – 221Combined sources3
Beta strandi222 – 226Combined sources5
Helixi231 – 249Combined sources19
Helixi274 – 287Combined sources14
Turni293 – 295Combined sources3
Helixi296 – 308Combined sources13
Beta strandi317 – 322Combined sources6
Helixi326 – 335Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7M523.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR001926. TrpB-like_PLP-dep.
[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

« Hide

        10         20         30         40         50
SGVAKFAKYP LTFGPSPISN LNRLSQHLGS KVNVYAKRED CNSGLAFGGN
60 70 80 90 100
KLRKLEYIVP DIVEGDYTHL VSIGGRQSNQ TRMVAALAAK LGKKCVLIQE
110 120 130 140 150
DWVPIPEAEK DVYNRVGNIE LSRIMGADVR VIEDGFDIGM RKSFANALQE
160 170 180 190 200
LEDAGHKPYP IPAGCSEHKY GGLGFVGFAD EVINQEVELG IKFDKIVVCC
210 220 230 240 250
VTGSTTAGIL AGMAQYGRQD DVIAIDASFT SEKTKEQTLR IANNTAKLIG
260 270 280 290 300
VEHEFKDFTL DTRFAYPCYG VPNEGTIEAI RTCAEQEGVL TDPVYEGKSM
310 320 330 340
QGLIALIKED YFKPGANVLY VHLGGAPALS AYSSFFPTKT A
Length:341
Mass (Da):37,061
Last modified:December 15, 2003 - v1
Checksum:i64904CDD7AA2C5FA
GO

Sequence databases

PIRiPW0041.

Cross-referencesi

Sequence databases

PIRiPW0041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.99.7. 2588.

Miscellaneous databases

EvolutionaryTraceiQ7M523.

Family and domain databases

InterProiIPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01274. ACC_deam. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 59 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.