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P07662

- G7AC_PSEU7

UniProt

P07662 - G7AC_PSEU7

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Protein

Glutaryl-7-aminocephalosporanic-acid acylase

Gene
N/A
Organism
Pseudomonas sp. (strain SY-77)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA).1 Publication

Catalytic activityi

(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei199 – 1991Nucleophile
Active sitei221 – 2211 Reviewed prediction
Active sitei653 – 6531 Reviewed prediction

GO - Molecular functioni

  1. glutaryl-7-aminocephalosporanic-acid acylase activity Source: UniProtKB-EC

GO - Biological processi

  1. antibiotic biosynthetic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Protein family/group databases

MEROPSiS45.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaryl-7-aminocephalosporanic-acid acylase (EC:3.5.1.93)
Short name:
Glutaryl-7-ACA acylase
Alternative name(s):
7-beta-(4-carboxybutanamido)cephalosporanic acid acylase
GL-7-ACA acylase
Short name:
GCA
Cleaved into the following 2 chains:
Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha
Short name:
Glutaryl-7-ACA acylase subunit alpha
Glutaryl-7-aminocephalosporanic-acid acylase subunit beta
Short name:
Glutaryl-7-ACA acylase subunit beta
OrganismiPseudomonas sp. (strain SY-77)
Taxonomic identifieri269086 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

Periplasm 1 Publication

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991S → A: Loss of activity. Lack of autoprocessing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 720691Glutaryl-7-aminocephalosporanic-acid acylasePRO_0000027353Add
BLAST
Chaini30 – 189160Glutaryl-7-aminocephalosporanic-acid acylase subunit alphaPRO_0000027354Add
BLAST
Propeptidei190 – 1989Spacer peptidePRO_0000253351
Chaini199 – 720522Glutaryl-7-aminocephalosporanic-acid acylase subunit betaPRO_0000027355Add
BLAST

Keywords - PTMi

Zymogen

Expressioni

Inductioni

By glutaric acid.1 Publication

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits processed from the same precursor.1 Publication

Structurei

Secondary structure

1
720
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 525
Beta strandi57 – 604
Helixi64 – 9027
Helixi94 – 985
Helixi100 – 1023
Helixi103 – 1119
Helixi114 – 12310
Helixi127 – 14620
Helixi148 – 1503
Helixi153 – 1586
Helixi163 – 17614
Turni177 – 1793
Helixi182 – 1865
Helixi192 – 1954
Beta strandi200 – 2045
Helixi206 – 2083
Beta strandi209 – 2124
Beta strandi215 – 2195
Beta strandi221 – 2255
Helixi227 – 2293
Beta strandi231 – 2377
Beta strandi242 – 2487
Beta strandi255 – 2584
Beta strandi260 – 2678
Beta strandi274 – 2785
Beta strandi285 – 2884
Beta strandi291 – 2933
Beta strandi299 – 3057
Beta strandi311 – 3177
Beta strandi322 – 3287
Beta strandi334 – 3407
Helixi347 – 3559
Helixi360 – 3678
Beta strandi376 – 3816
Beta strandi386 – 3905
Helixi402 – 4065
Beta strandi407 – 4126
Helixi414 – 4163
Helixi424 – 4263
Beta strandi429 – 4324
Beta strandi436 – 4394
Beta strandi441 – 4433
Beta strandi448 – 4514
Helixi456 – 4583
Helixi471 – 48111
Helixi488 – 4958
Helixi501 – 51414
Helixi520 – 53112
Helixi543 – 55311
Turni555 – 5584
Beta strandi564 – 5663
Turni573 – 5753
Beta strandi577 – 5815
Helixi583 – 60119
Beta strandi602 – 6054
Helixi608 – 6114
Beta strandi612 – 6165
Beta strandi619 – 6224
Helixi628 – 6303
Beta strandi633 – 6386
Beta strandi649 – 6535
Beta strandi655 – 6606
Beta strandi666 – 6716
Beta strandi682 – 6876
Helixi688 – 6914
Turni692 – 6943
Helixi703 – 7097
Beta strandi710 – 7156

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GK0X-ray2.50A/C36-188[»]
B/D199-720[»]
1GK1X-ray2.40A/C36-188[»]
B/D199-720[»]
1OR0X-ray2.00A/C30-189[»]
B/D199-720[»]
2ADVX-ray2.24A30-195[»]
B199-226[»]
C227-720[»]
2AE3X-ray2.40A30-195[»]
B199-720[»]
2AE4X-ray2.30A30-195[»]
B199-720[»]
2AE5X-ray2.24A30-195[»]
B200-720[»]
3S8RX-ray2.50A/B30-720[»]
ProteinModelPortaliP07662.
SMRiP07662. Positions 35-720.

Miscellaneous databases

EvolutionaryTraceiP07662.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S45 family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.439.10. 1 hit.
3.60.20.10. 2 hits.
InterProiIPR029055. Ntn_hydrolases_N.
IPR014395. Pen/cephalosporin_acylase.
IPR002692. Penicillin_amidase-like.
IPR023343. Penicillin_amidase_dom1.
[Graphical view]
PfamiPF01804. Penicil_amidase. 2 hits.
[Graphical view]
PIRSFiPIRSF001227. Pen_acylase. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P07662-1 [UniParc]FASTAAdd to Basket

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MLRVLHRAAS ALVMATVIGL APAVAFALAE PTSTPQAPIA AYKPRSNEIL    50
WDGYGVPHIY GVDAPSAFYG YGWAQARSHG DNILRLYGEA RGKGAEYWGP 100
DYEQTTVWLL TNGVPERAQQ WYAQQSPDFR ANLDAFAAGI NAYAQQNPDD 150
ISPEVRQVLP VSGADVVAHA HRLMNFLYVA SPGRTLGEGD PPDLADQGSN 200
SWAVAPGKTA NGNALLLQNP HLSWTTDYFT YYEAHLVTPD FEIYGATQIG 250
LPVIRFAFNQ RMGITNTVNG MVGATNYRLT LQDGGYLYDG QVRPFERPQA 300
SYRLRQADGT TVDKPLEIRS SVHGPVFERA DGTAVAVRVA GLDRPGMLEQ 350
YFDMITADSF DDYEAALARM QVPTFNIVYA DREGTINYSF NGVAPKRAEG 400
DIAFWQGLVP GDSSRYLWTE THPLDDLPRV TNPPGGFVQN SNDPPWTPTW 450
PVTYTPKDFP SYLAPQTPHS LRAQQSVRLM SENDDLTLER FMALQLSHRA 500
VMADRTLPDL IPAALIDPDP EVQAAARLLA AWDREFTSDS RAALLFEEWA 550
RLFAGQNFAG QAGFATPWSL DKPVSTPYGV RDPKAAVDQL RTAIANTKRK 600
YGAIDRPFGD ASRMILNDVN VPGAAGYGNL GSFRVFTWSD PDENGVRTPV 650
HGETWVAMIE FSTPVRAYGL MSYGNSRQPG TTHYSDQIER VSRADFRELL 700
LRREQVEAAV QERTPFNFKP 720
Length:720
Mass (Da):79,627
Last modified:October 17, 2006 - v2
Checksum:i643250675A266C33
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791H → Q in AAA25826. 1 Publication
Sequence conflicti154 – 1541E → D in AAA25826. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF458663 Genomic DNA. Translation: AAN39264.1.
M11436 Genomic DNA. Translation: AAA25826.1.
PIRiA24928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF458663 Genomic DNA. Translation: AAN39264.1 .
M11436 Genomic DNA. Translation: AAA25826.1 .
PIRi A24928.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GK0 X-ray 2.50 A/C 36-188 [» ]
B/D 199-720 [» ]
1GK1 X-ray 2.40 A/C 36-188 [» ]
B/D 199-720 [» ]
1OR0 X-ray 2.00 A/C 30-189 [» ]
B/D 199-720 [» ]
2ADV X-ray 2.24 A 30-195 [» ]
B 199-226 [» ]
C 227-720 [» ]
2AE3 X-ray 2.40 A 30-195 [» ]
B 199-720 [» ]
2AE4 X-ray 2.30 A 30-195 [» ]
B 199-720 [» ]
2AE5 X-ray 2.24 A 30-195 [» ]
B 200-720 [» ]
3S8R X-ray 2.50 A/B 30-720 [» ]
ProteinModelPortali P07662.
SMRi P07662. Positions 35-720.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S45.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P07662.

Family and domain databases

Gene3Di 1.10.439.10. 1 hit.
3.60.20.10. 2 hits.
InterProi IPR029055. Ntn_hydrolases_N.
IPR014395. Pen/cephalosporin_acylase.
IPR002692. Penicillin_amidase-like.
IPR023343. Penicillin_amidase_dom1.
[Graphical view ]
Pfami PF01804. Penicil_amidase. 2 hits.
[Graphical view ]
PIRSFi PIRSF001227. Pen_acylase. 1 hit.
SUPFAMi SSF56235. SSF56235. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Directed evolution of a glutaryl acylase into an adipyl acylase."
    Sio C.F., Riemens A.M., Van Der Laan J.M., Verhaert R.M., Quax W.J.
    Eur. J. Biochem. 269:4495-4504(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and structure of the gene for 7 beta-(4-carboxybutanamido)cephalosporanic acid acylase from a Pseudomonas strain."
    Matsuda A., Komatsu K.
    J. Bacteriol. 163:1222-1228(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-311, PROTEIN SEQUENCE OF 30-46 AND 199-215, FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  3. "Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation."
    Kim J.K., Yang I.S., Rhee S., Dauter Z., Lee Y.S., Park S.S., Kim K.H.
    Biochemistry 42:4084-4093(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-189 AND 199-720 OF WILD-TYPE AND 30-720 OF MUTANT ALA-199, SUBUNIT, MUTAGENESIS OF SER-199, AUTOCATALYTIC PROCESSING MECHANISM.

Entry informationi

Entry nameiG7AC_PSEU7
AccessioniPrimary (citable) accession number: P07662
Secondary accession number(s): Q84I62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 83 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

External Data

Dasty 3

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