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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei78 – 781NucleophileUniRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3383381-aminocyclopropane-1-carboxylate deaminasePRO_0000184505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi12 – 154Combined sources
Beta strandi18 – 203Combined sources
Helixi22 – 276Combined sources
Beta strandi30 – 389Combined sources
Helixi39 – 413Combined sources
Helixi50 – 567Combined sources
Helixi59 – 646Combined sources
Beta strandi69 – 757Combined sources
Helixi79 – 9113Combined sources
Beta strandi94 – 1007Combined sources
Turni108 – 1125Combined sources
Helixi114 – 1218Combined sources
Beta strandi125 – 1284Combined sources
Helixi135 – 1384Combined sources
Helixi140 – 15011Combined sources
Beta strandi155 – 1573Combined sources
Helixi160 – 1623Combined sources
Turni166 – 1694Combined sources
Helixi171 – 18616Combined sources
Beta strandi191 – 20010Combined sources
Helixi201 – 21111Combined sources
Turni212 – 2143Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2235Combined sources
Helixi228 – 24619Combined sources
Helixi254 – 2563Combined sources
Beta strandi258 – 2603Combined sources
Helixi273 – 28614Combined sources
Turni292 – 2943Combined sources
Helixi295 – 30713Combined sources
Beta strandi316 – 3216Combined sources
Helixi325 – 3317Combined sources
Helixi333 – 3353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-338.
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
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. Positions 1-338.
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: October 14, 2015
This is version 75 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.