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Protein

Penicillin acylase

Gene
N/A
Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The enzyme catalyzes the conversion of penicillin to 6-aminopenicillanate The precursor, furthermore, acts as a self-processing peptidase that cleaves off the propeptide. All peptidase activity is lost on conversion to the mature peptidase.

Catalytic activityi

Penicillin + H2O = a carboxylate + 6-aminopenicillanate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei41

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Protein family/group databases

MEROPSiC59.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin acylase (EC:3.5.1.11)
Alternative name(s):
Penicillin V amidase
Short name:
PVA
OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifieri1421 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

Pathology & Biotechi

Chemistry databases

DrugBankiDB00417. Phenoxymethylpenicillin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000452781 – 3Removed in mature form1 Publication3
ChainiPRO_00000452794 – 338Penicillin acylaseAdd BLAST335

Keywords - PTMi

Zymogen

Miscellaneous databases

PMAP-CutDBP12256.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi16 – 26Combined sources11
Beta strandi31 – 35Combined sources5
Beta strandi41 – 43Combined sources3
Beta strandi45 – 47Combined sources3
Beta strandi50 – 52Combined sources3
Beta strandi57 – 62Combined sources6
Beta strandi64 – 67Combined sources4
Beta strandi69 – 75Combined sources7
Beta strandi80 – 85Combined sources6
Turni87 – 89Combined sources3
Beta strandi93 – 95Combined sources3
Beta strandi101 – 103Combined sources3
Helixi105 – 107Combined sources3
Helixi108 – 115Combined sources8
Helixi119 – 127Combined sources9
Beta strandi129 – 132Combined sources4
Turni137 – 139Combined sources3
Beta strandi145 – 150Combined sources6
Beta strandi156 – 162Combined sources7
Beta strandi165 – 169Combined sources5
Beta strandi174 – 176Combined sources3
Beta strandi178 – 180Combined sources3
Helixi182 – 188Combined sources7
Helixi189 – 192Combined sources4
Beta strandi203 – 205Combined sources3
Beta strandi208 – 210Combined sources3
Beta strandi213 – 215Combined sources3
Helixi217 – 219Combined sources3
Helixi228 – 241Combined sources14
Helixi248 – 260Combined sources13
Beta strandi268 – 270Combined sources3
Beta strandi278 – 286Combined sources9
Turni287 – 290Combined sources4
Beta strandi291 – 296Combined sources6
Beta strandi299 – 307Combined sources9
Beta strandi318 – 321Combined sources4
Beta strandi329 – 331Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IWMX-ray2.50A/B/C/D1-338[»]
2PVAX-ray2.50A/B/C/D4-338[»]
2QUYX-ray1.70A/B/C/D/E/F/G/H4-338[»]
2Z71X-ray2.60A/C4-338[»]
3MJIX-ray2.50A/B/C/D1-338[»]
3PVAX-ray2.80A/B/C/D/E/F/G/H4-338[»]
ProteinModelPortaliP12256.
SMRiP12256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12256.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C59 family.Curated

Family and domain databases

Gene3Di3.60.60.10. 1 hit.
InterProiIPR029132. CBAH/NAAA_C.
IPR003199. Chologlycine_hydro/PeptC59.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGCSSLSIR TTDDKSLFAR TMDFTMEPDS KVIIVPRNYG IRLLEKENVV
60 70 80 90 100
INNSYAFVGM GSTDITSPVL YDGVNEKGLM GAMLYYATFA TYADEPKKGT
110 120 130 140 150
TGINPVYVIS QVLGNCVTVD DVIEKLTSYT LLNEANIILG FAPPLHYTFT
160 170 180 190 200
DASGESIVIE PDKTGITIHR KTIGVMTNSP GYEWHQTNLR AYIGVTPNPP
210 220 230 240 250
QDIMMGDLDL TPFGQGAGGL GLPGDFTPSA RFLRVAYWKK YTEKAKNETE
260 270 280 290 300
GVTNLFHILS SVNIPKGVVL TNEGKTDYTI YTSAMCAQSK NYYFKLYDNS
310 320 330
RISAVSLMAE NLNSQDLITF EWDRKQDIKQ LNQVNVMS
Length:338
Mass (Da):37,458
Last modified:October 1, 1989 - v1
Checksum:i69C8A9F69BB084B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15660 Genomic DNA. Translation: AAA22654.1.
PIRiA25559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15660 Genomic DNA. Translation: AAA22654.1.
PIRiA25559.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IWMX-ray2.50A/B/C/D1-338[»]
2PVAX-ray2.50A/B/C/D4-338[»]
2QUYX-ray1.70A/B/C/D/E/F/G/H4-338[»]
2Z71X-ray2.60A/C4-338[»]
3MJIX-ray2.50A/B/C/D1-338[»]
3PVAX-ray2.80A/B/C/D/E/F/G/H4-338[»]
ProteinModelPortaliP12256.
SMRiP12256.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB00417. Phenoxymethylpenicillin.

Protein family/group databases

MEROPSiC59.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP12256.
PMAP-CutDBP12256.

Family and domain databases

Gene3Di3.60.60.10. 1 hit.
InterProiIPR029132. CBAH/NAAA_C.
IPR003199. Chologlycine_hydro/PeptC59.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPAC_LYSSH
AccessioniPrimary (citable) accession number: P12256
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 84 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. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.