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P07662

- G7AC_PSEU7

UniProt

P07662 - G7AC_PSEU7

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
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    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

    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

    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 – 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.
    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

    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

    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:
    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: October 1, 2014
    This is version 84 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