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Protein

1-aminocyclopropane-1-carboxylate deaminase

Gene

acdS

Organism
Pseudomonas sp. (strain ACP)
Status
Reviewed-Annotation score: Annotation score: 3 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. Allows growth on ACC as a nitrogen source.UniRule annotation1 Publication

Catalytic activityi

1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3.UniRule annotation1 Publication

Cofactori

pyridoxal 5'-phosphateUniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei78NucleophileUniRule annotation1

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. 5085.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate deaminaseUniRule annotation (EC:3.5.99.7UniRule annotation)
Short name:
ACC deaminaseUniRule annotation
Short name:
ACCDUniRule annotation
Gene namesi
Name:acdSUniRule annotation
OrganismiPseudomonas sp. (strain ACP)
Taxonomic identifieri74568 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001845051 – 3381-aminocyclopropane-1-carboxylate deaminaseAdd BLAST338

Amino acid modifications

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

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi12 – 15Combined sources4
Beta strandi18 – 20Combined sources3
Helixi22 – 27Combined sources6
Beta strandi30 – 38Combined sources9
Helixi39 – 41Combined sources3
Helixi50 – 56Combined sources7
Helixi59 – 64Combined sources6
Beta strandi69 – 75Combined sources7
Helixi79 – 91Combined sources13
Beta strandi94 – 100Combined sources7
Turni108 – 112Combined sources5
Helixi114 – 121Combined sources8
Beta strandi125 – 128Combined sources4
Helixi135 – 138Combined sources4
Helixi140 – 150Combined sources11
Beta strandi155 – 157Combined sources3
Helixi160 – 162Combined sources3
Turni166 – 169Combined sources4
Helixi171 – 186Combined sources16
Beta strandi191 – 200Combined sources10
Helixi201 – 211Combined sources11
Turni212 – 214Combined sources3
Helixi216 – 218Combined sources3
Beta strandi219 – 223Combined sources5
Helixi228 – 246Combined sources19
Helixi254 – 256Combined sources3
Beta strandi258 – 260Combined sources3
Helixi273 – 286Combined sources14
Turni292 – 294Combined sources3
Helixi295 – 307Combined sources13
Beta strandi316 – 321Combined sources6
Helixi325 – 331Combined sources7
Helixi333 – 335Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RQXX-ray2.50A/B/C/D1-338[»]
1TYZX-ray2.00A/B/C/D1-338[»]
1TZ2X-ray2.10A/B/C/D1-338[»]
1TZJX-ray1.99A/B/C/D1-338[»]
1TZKX-ray2.00A/B/C/D1-338[»]
1TZMX-ray2.08A/B/C/D1-338[»]
ProteinModelPortaliQ00740.
SMRiQ00740.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00740.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

HAMAPiMF_00807. ACC_deaminase. 1 hit.
InterProiIPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR020601. ACP_carboxylate_deaminase_bac.
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.

Q00740-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLQRFPRYP LTFGPTPIQP LARLSKHLGG KVHLYAKRED CNSGLAFGGN
60 70 80 90 100
KTRKLEYLIP EALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE
110 120 130 140 150
NWVNYSDAVY DRVGNIQMSR ILGADVRLVP DGFDIGFRRS WEDALESVRA
160 170 180 190 200
AGGKPYAIPA GCSDHPLGGL GFVGFAEEVR AQEAELGFKF DYVVVCSVTG
210 220 230 240 250
STQAGMVVGF AADGRADRVI GVDASAKPAQ TREQITRIAR QTAEKVGLER
260 270 280 290 300
DIMRADVVLD ERFAGPEYGL PNEGTLEAIR LCARTEGMLT DPVYEGKSMH
310 320 330
GMIEMVRNGE FPEGSRVLYA HLGGVPALNG YSFIFRDG
Length:338
Mass (Da):36,672
Last modified:April 1, 1993 - v1
Checksum:i01FC286177012FDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73488 Genomic DNA. Translation: AAA25689.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73488 Genomic DNA. Translation: AAA25689.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RQXX-ray2.50A/B/C/D1-338[»]
1TYZX-ray2.00A/B/C/D1-338[»]
1TZ2X-ray2.10A/B/C/D1-338[»]
1TZJX-ray1.99A/B/C/D1-338[»]
1TZKX-ray2.00A/B/C/D1-338[»]
1TZMX-ray2.08A/B/C/D1-338[»]
ProteinModelPortaliQ00740.
SMRiQ00740.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.99.7. 5085.

Miscellaneous databases

EvolutionaryTraceiQ00740.

Family and domain databases

HAMAPiMF_00807. ACC_deaminase. 1 hit.
InterProiIPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR020601. ACP_carboxylate_deaminase_bac.
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_PSEUD
AccessioniPrimary (citable) accession number: Q00740
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.