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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 – 2211Sequence Analysis
Active sitei653 – 6531Sequence Analysis

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-KW
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 peptide1 PublicationPRO_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 – 525Combined sources
Beta strandi57 – 604Combined sources
Helixi64 – 9027Combined sources
Helixi94 – 985Combined sources
Helixi100 – 1023Combined sources
Helixi103 – 1119Combined sources
Helixi114 – 12310Combined sources
Helixi127 – 14620Combined sources
Helixi148 – 1503Combined sources
Helixi153 – 1586Combined sources
Helixi163 – 17614Combined sources
Turni177 – 1793Combined sources
Helixi182 – 1865Combined sources
Helixi192 – 1954Combined sources
Beta strandi200 – 2045Combined sources
Helixi206 – 2083Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi221 – 2255Combined sources
Helixi227 – 2293Combined sources
Beta strandi231 – 2377Combined sources
Beta strandi242 – 2487Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi260 – 2678Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi299 – 3057Combined sources
Beta strandi311 – 3177Combined sources
Beta strandi322 – 3287Combined sources
Beta strandi334 – 3407Combined sources
Helixi347 – 3559Combined sources
Helixi360 – 3678Combined sources
Beta strandi376 – 3816Combined sources
Beta strandi386 – 3905Combined sources
Helixi402 – 4065Combined sources
Beta strandi407 – 4126Combined sources
Helixi414 – 4163Combined sources
Helixi424 – 4263Combined sources
Beta strandi429 – 4324Combined sources
Beta strandi436 – 4394Combined sources
Beta strandi441 – 4433Combined sources
Beta strandi448 – 4514Combined sources
Helixi456 – 4583Combined sources
Helixi471 – 48111Combined sources
Helixi488 – 4958Combined sources
Helixi501 – 51414Combined sources
Helixi520 – 53112Combined sources
Helixi543 – 55311Combined sources
Turni555 – 5584Combined sources
Beta strandi564 – 5663Combined sources
Turni573 – 5753Combined sources
Beta strandi577 – 5815Combined sources
Helixi583 – 60119Combined sources
Beta strandi602 – 6054Combined sources
Helixi608 – 6114Combined sources
Beta strandi612 – 6165Combined sources
Beta strandi619 – 6224Combined sources
Helixi628 – 6303Combined sources
Beta strandi633 – 6386Combined sources
Beta strandi649 – 6535Combined sources
Beta strandi655 – 6606Combined sources
Beta strandi666 – 6716Combined sources
Beta strandi682 – 6876Combined sources
Helixi688 – 6914Combined sources
Turni692 – 6943Combined sources
Helixi703 – 7097Combined sources
Beta strandi710 – 7156Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07662.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S45 family.Curated

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

« Hide

        10         20         30         40         50
MLRVLHRAAS ALVMATVIGL APAVAFALAE PTSTPQAPIA AYKPRSNEIL
60 70 80 90 100
WDGYGVPHIY GVDAPSAFYG YGWAQARSHG DNILRLYGEA RGKGAEYWGP
110 120 130 140 150
DYEQTTVWLL TNGVPERAQQ WYAQQSPDFR ANLDAFAAGI NAYAQQNPDD
160 170 180 190 200
ISPEVRQVLP VSGADVVAHA HRLMNFLYVA SPGRTLGEGD PPDLADQGSN
210 220 230 240 250
SWAVAPGKTA NGNALLLQNP HLSWTTDYFT YYEAHLVTPD FEIYGATQIG
260 270 280 290 300
LPVIRFAFNQ RMGITNTVNG MVGATNYRLT LQDGGYLYDG QVRPFERPQA
310 320 330 340 350
SYRLRQADGT TVDKPLEIRS SVHGPVFERA DGTAVAVRVA GLDRPGMLEQ
360 370 380 390 400
YFDMITADSF DDYEAALARM QVPTFNIVYA DREGTINYSF NGVAPKRAEG
410 420 430 440 450
DIAFWQGLVP GDSSRYLWTE THPLDDLPRV TNPPGGFVQN SNDPPWTPTW
460 470 480 490 500
PVTYTPKDFP SYLAPQTPHS LRAQQSVRLM SENDDLTLER FMALQLSHRA
510 520 530 540 550
VMADRTLPDL IPAALIDPDP EVQAAARLLA AWDREFTSDS RAALLFEEWA
560 570 580 590 600
RLFAGQNFAG QAGFATPWSL DKPVSTPYGV RDPKAAVDQL RTAIANTKRK
610 620 630 640 650
YGAIDRPFGD ASRMILNDVN VPGAAGYGNL GSFRVFTWSD PDENGVRTPV
660 670 680 690 700
HGETWVAMIE FSTPVRAYGL MSYGNSRQPG TTHYSDQIER VSRADFRELL
710 720
LRREQVEAAV QERTPFNFKP
Length:720
Mass (Da):79,627
Last modified:October 17, 2006 - v2
Checksum:i643250675A266C33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791H → Q in AAA25826. (PubMed:2993240)Curated
Sequence conflicti154 – 1541E → D in AAA25826. (PubMed:2993240)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458663 Genomic DNA. Translation: AAN39264.1.
M11436 Genomic DNA. Translation: AAA25826.1.
PIRiA24928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458663 Genomic DNA. Translation: AAN39264.1 .
M11436 Genomic DNA. Translation: AAA25826.1 .
PIRi A24928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 86 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