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Protein

Penicillin G acylase

Gene

pac

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Penicillin + H2O = a carboxylate + 6-aminopenicillanate.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per dimer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi178Calcium1
Active sitei290Nucleophile1
Metal bindingi362Calcium1
Metal bindingi364Calcium; via carbonyl oxygen1
Metal bindingi365Calcium1
Metal bindingi494Calcium; via carbonyl oxygen1
Metal bindingi541Calcium1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18775.
BRENDAi3.5.1.11. 2026.
SABIO-RKP06875.

Protein family/group databases

MEROPSiS45.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin G acylase (EC:3.5.1.11)
Alternative name(s):
Penicillin G amidase
Penicillin G amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:pac
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi290S → C: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000002734527 – 846Penicillin G acylaseAdd BLAST820
ChainiPRO_000002734627 – 235Penicillin G acylase subunit alphaAdd BLAST209
PropeptideiPRO_0000027347236 – 289Spacer peptideAdd BLAST54
ChainiPRO_0000027348290 – 846Penicillin G acylase subunit betaAdd BLAST557

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiP06875.

Interactioni

Subunit structurei

Heterodimer of an alpha subunit and a beta subunit processed from the same precursor.

Structurei

Secondary structure

1846
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 38Combined sources7
Beta strandi43 – 46Combined sources4
Helixi50 – 77Combined sources28
Helixi81 – 84Combined sources4
Helixi86 – 88Combined sources3
Helixi89 – 97Combined sources9
Helixi101 – 109Combined sources9
Helixi113 – 135Combined sources23
Helixi137 – 140Combined sources4
Helixi143 – 148Combined sources6
Helixi157 – 167Combined sources11
Helixi169 – 172Combined sources4
Helixi178 – 192Combined sources15
Helixi194 – 204Combined sources11
Beta strandi214 – 216Combined sources3
Turni218 – 220Combined sources3
Helixi229 – 231Combined sources3
Helixi232 – 234Combined sources3
Helixi235 – 237Combined sources3
Helixi246 – 249Combined sources4
Helixi264 – 278Combined sources15
Helixi279 – 281Combined sources3
Beta strandi291 – 295Combined sources5
Turni297 – 299Combined sources3
Beta strandi300 – 310Combined sources11
Beta strandi316 – 318Combined sources3
Beta strandi320 – 328Combined sources9
Beta strandi331 – 338Combined sources8
Beta strandi345 – 348Combined sources4
Beta strandi350 – 358Combined sources9
Beta strandi364 – 370Combined sources7
Beta strandi373 – 375Combined sources3
Beta strandi378 – 381Combined sources4
Beta strandi384 – 387Combined sources4
Beta strandi389 – 395Combined sources7
Beta strandi403 – 410Combined sources8
Beta strandi413 – 419Combined sources7
Turni420 – 423Combined sources4
Beta strandi424 – 430Combined sources7
Turni431 – 434Combined sources4
Helixi436 – 445Combined sources10
Helixi446 – 448Combined sources3
Helixi452 – 459Combined sources8
Beta strandi464 – 472Combined sources9
Beta strandi477 – 483Combined sources7
Beta strandi498 – 502Combined sources5
Helixi512 – 514Combined sources3
Beta strandi517 – 520Combined sources4
Beta strandi524 – 530Combined sources7
Beta strandi532 – 534Combined sources3
Helixi553 – 561Combined sources9
Beta strandi562 – 564Combined sources3
Helixi568 – 580Combined sources13
Helixi585 – 596Combined sources12
Helixi604 – 613Combined sources10
Beta strandi625 – 630Combined sources6
Helixi632 – 646Combined sources15
Helixi648 – 651Combined sources4
Helixi656 – 660Combined sources5
Helixi680 – 689Combined sources10
Helixi690 – 693Combined sources4
Beta strandi694 – 696Combined sources3
Turni702 – 705Combined sources4
Helixi708 – 727Combined sources20
Helixi731 – 733Combined sources3
Beta strandi741 – 746Combined sources6
Beta strandi752 – 754Combined sources3
Helixi756 – 758Combined sources3
Beta strandi760 – 764Combined sources5
Beta strandi770 – 778Combined sources9
Beta strandi780 – 783Combined sources4
Beta strandi785 – 791Combined sources7
Beta strandi810 – 813Combined sources4
Helixi814 – 818Combined sources5
Beta strandi823 – 825Combined sources3
Helixi829 – 834Combined sources6
Beta strandi836 – 843Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AI4X-ray2.35A27-235[»]
B290-846[»]
1AI5X-ray2.36A27-235[»]
B290-846[»]
1AI6X-ray2.55A27-235[»]
B290-846[»]
1AI7X-ray2.50A27-235[»]
B290-846[»]
1AJNX-ray2.36A27-235[»]
B290-846[»]
1AJPX-ray2.31A27-235[»]
B290-846[»]
1AJQX-ray2.05A27-235[»]
B290-846[»]
1E3AX-ray1.80A27-286[»]
B287-846[»]
1FXHX-ray1.97A27-235[»]
B290-846[»]
1FXVX-ray2.25A27-235[»]
B290-846[»]
1GK9X-ray1.30A27-286[»]
B290-846[»]
1GKFX-ray1.41A27-286[»]
B290-846[»]
1GM7X-ray1.45A27-235[»]
B290-846[»]
1GM8X-ray2.00A27-235[»]
B290-846[»]
1GM9X-ray1.80A27-235[»]
B290-846[»]
1H2GX-ray2.00A27-235[»]
B290-846[»]
1JX9X-ray2.28A26-234[»]
B290-846[»]
1K5QX-ray2.34A26-234[»]
B290-846[»]
1K5SX-ray2.43A26-234[»]
B290-846[»]
1K7DX-ray2.15A26-234[»]
B290-846[»]
1KECX-ray2.30A26-234[»]
B290-846[»]
1PNKX-ray1.90A27-235[»]
B290-846[»]
1PNLX-ray2.50A27-235[»]
B290-846[»]
1PNMX-ray2.50A27-235[»]
B290-846[»]
ProteinModelPortaliP06875.
SMRiP06875.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06875.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S45 family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd03748. Ntn_PGA. 1 hit.
Gene3Di1.10.439.10. 1 hit.
3.60.20.10. 2 hits.
InterProiIPR029055. Ntn_hydrolases_N.
IPR002692. Pen/cephal_acylase.
IPR014395. Pen_acylase.
IPR023343. Penicillin_amidase_dom1.
IPR033813. PGA_C.
[Graphical view]
PfamiPF01804. Penicil_amidase. 1 hit.
[Graphical view]
PIRSFiPIRSF001227. Pen_acylase. 1 hit.
SUPFAMiSSF56235. SSF56235. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P06875-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNRNRMIVN CVTASLMYYW SLPALAEQSS SEIKIVRDEY GMPHIYANDT
60 70 80 90 100
WHLFYGYGYV VAQDRLFQME MARRSTQGTV AEVLGKDFVK FDKDIRRNYW
110 120 130 140 150
PDAIRAQIAA LSPEDMSILQ GYADGMNAWI DKVNTNPETL LPKQFNTFGF
160 170 180 190 200
TPKRWEPFDV AMIFVGTMAN RFSDSTSEID NLALLTALKD KYGVSQGMAV
210 220 230 240 250
FNQLKWLVNP SAPTTIAVQE SNYPLKFNQQ NSQTAALLPR YDLPAPMLDR
260 270 280 290 300
PAKGADGALL ALTAGKNRET IAAQFAQGGA NGLAGYPTTS NMWVIGKSKA
310 320 330 340 350
QDAKAIMVNG PQFGWYAPAY TYGIGLHGAG YDVTGNTPFA YPGLVFGHNG
360 370 380 390 400
VISWGSTAGF GDDVDIFAER LSAEKPGYYL HNGKWVKMLS REETITVKNG
410 420 430 440 450
QAETFTVWRT VHGNILQTDQ TTQTAYAKSR AWDGKEVASL LAWTHQMKAK
460 470 480 490 500
NWQEWTQQAA KQALTINWYY ADVNGNIGYV HTGAYPDRQS GHDPRLPVPG
510 520 530 540 550
TGKWDWKGLL PFEMNPKVYN PQSGYIANWN NSPQKDYPAS DLFAFLWGGA
560 570 580 590 600
DRVTEIDRLL EQKPRLTADQ AWDVIRQTSR QDLNLRLFLP TLQAATSGLT
610 620 630 640 650
QSDPRRQLVE TLTRWDGINL LNDDGKTWQQ PGSAILNVWL TSMLKRTVVA
660 670 680 690 700
AVPMPFDKWY SASGYETTQD GPTGSLNISV GAKILYEAVQ GDKSPIPQAV
710 720 730 740 750
DLFAGKPQQE VVLAALEDTW ETLSKRYGNN VSNWKTPAMA LTFRANNFFG
760 770 780 790 800
VPQAAAEETR HQAEYQNRGT ENDMIVFSPT TSDRPVLAWD VVAPGQSGFI
810 820 830 840
APDGTVDKHY EDQLKMYENF GRKSLWLTKQ DVEAHKESQE VLHVQR
Length:846
Mass (Da):94,643
Last modified:July 1, 1989 - v2
Checksum:i48570EDCB53BA227
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68Q → R in AAA24258 (PubMed:2989404).Curated1
Sequence conflicti77Q → R in AAA24258 (PubMed:2989404).Curated1
Sequence conflicti97R → S in AAA24258 (PubMed:2989404).Curated1
Sequence conflicti103A → R in AAA24270 (PubMed:3005131).Curated1
Sequence conflicti130I → T (PubMed:3315861).Curated1
Sequence conflicti130I → T (PubMed:2989404).Curated1
Sequence conflicti217A → G in AAA24258 (PubMed:2989404).Curated1
Sequence conflicti250R → P in AAA24270 (PubMed:3005131).Curated1
Sequence conflicti272A → V (PubMed:3016663).Curated1
Sequence conflicti272A → V (PubMed:2989404).Curated1
Sequence conflicti305A → R in AAA24270 (PubMed:3005131).Curated1
Sequence conflicti342 – 350PGLVFGHNG → LGWFPGYMV in AAA24258 (PubMed:2989404).Curated9
Sequence conflicti632G → P in AAA24324 (PubMed:3315861).Curated1
Sequence conflicti789W → Q in AAA24259 (PubMed:2989404).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15950 Genomic DNA. Translation: AAA24269.1.
X04114 Genomic DNA. Translation: CAA27728.1.
M17609 Genomic DNA. Translation: AAA24324.1.
M14424 Genomic DNA. Translation: AAA24270.1.
M11672 Genomic DNA. Translation: AAA24258.1.
M12373 Genomic DNA. Translation: AAA24259.1.
AF109125 Genomic DNA. Translation: AAD19653.1.
PIRiA23593. PNECA.
RefSeqiWP_000797400.1. NZ_MBPT01000022.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15950 Genomic DNA. Translation: AAA24269.1.
X04114 Genomic DNA. Translation: CAA27728.1.
M17609 Genomic DNA. Translation: AAA24324.1.
M14424 Genomic DNA. Translation: AAA24270.1.
M11672 Genomic DNA. Translation: AAA24258.1.
M12373 Genomic DNA. Translation: AAA24259.1.
AF109125 Genomic DNA. Translation: AAD19653.1.
PIRiA23593. PNECA.
RefSeqiWP_000797400.1. NZ_MBPT01000022.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AI4X-ray2.35A27-235[»]
B290-846[»]
1AI5X-ray2.36A27-235[»]
B290-846[»]
1AI6X-ray2.55A27-235[»]
B290-846[»]
1AI7X-ray2.50A27-235[»]
B290-846[»]
1AJNX-ray2.36A27-235[»]
B290-846[»]
1AJPX-ray2.31A27-235[»]
B290-846[»]
1AJQX-ray2.05A27-235[»]
B290-846[»]
1E3AX-ray1.80A27-286[»]
B287-846[»]
1FXHX-ray1.97A27-235[»]
B290-846[»]
1FXVX-ray2.25A27-235[»]
B290-846[»]
1GK9X-ray1.30A27-286[»]
B290-846[»]
1GKFX-ray1.41A27-286[»]
B290-846[»]
1GM7X-ray1.45A27-235[»]
B290-846[»]
1GM8X-ray2.00A27-235[»]
B290-846[»]
1GM9X-ray1.80A27-235[»]
B290-846[»]
1H2GX-ray2.00A27-235[»]
B290-846[»]
1JX9X-ray2.28A26-234[»]
B290-846[»]
1K5QX-ray2.34A26-234[»]
B290-846[»]
1K5SX-ray2.43A26-234[»]
B290-846[»]
1K7DX-ray2.15A26-234[»]
B290-846[»]
1KECX-ray2.30A26-234[»]
B290-846[»]
1PNKX-ray1.90A27-235[»]
B290-846[»]
1PNLX-ray2.50A27-235[»]
B290-846[»]
1PNMX-ray2.50A27-235[»]
B290-846[»]
ProteinModelPortaliP06875.
SMRiP06875.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS45.001.

Proteomic databases

PRIDEiP06875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18775.
BRENDAi3.5.1.11. 2026.
SABIO-RKP06875.

Miscellaneous databases

EvolutionaryTraceiP06875.

Family and domain databases

CDDicd03748. Ntn_PGA. 1 hit.
Gene3Di1.10.439.10. 1 hit.
3.60.20.10. 2 hits.
InterProiIPR029055. Ntn_hydrolases_N.
IPR002692. Pen/cephal_acylase.
IPR014395. Pen_acylase.
IPR023343. Penicillin_amidase_dom1.
IPR033813. PGA_C.
[Graphical view]
PfamiPF01804. Penicil_amidase. 1 hit.
[Graphical view]
PIRSFiPIRSF001227. Pen_acylase. 1 hit.
SUPFAMiSSF56235. SSF56235. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiPAC_ECOLX
AccessioniPrimary (citable) accession number: P06875
Secondary accession number(s): Q47434
, Q47435, Q47436, Q47437, Q60253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 118 of the entry and version 2 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.