Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutaryl-7-aminocephalosporanic-acid acylase

Gene
N/A
Organism
Brevundimonas diminuta (Pseudomonas diminuta)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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). Cannot efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as substrates.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei199Nucleophile1
Active sitei221Sequence analysis1
Active sitei653Sequence analysis1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processAntibiotic resistance

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.93 982

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S45.002

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
CAD
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBrevundimonas diminuta (Pseudomonas diminuta)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri293 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeBrevundimonas

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 29By similarityAdd BLAST29
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002735630 – 720Glutaryl-7-aminocephalosporanic-acid acylaseAdd BLAST691
ChainiPRO_000025378230 – 187Glutaryl-7-aminocephalosporanic-acid acylase subunit alphaAdd BLAST158
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000253783188 – 198Spacer peptideAdd BLAST11
ChainiPRO_0000253784199 – 720Glutaryl-7-aminocephalosporanic-acid acylase subunit betaAdd BLAST522

Keywords - PTMi

Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9L5D6

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of a small subunit and a large subunit processed from the same precursor.1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1720
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9L5D6

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9L5D6

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9L5D6

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S45 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K12748

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.439.10, 1 hit
3.60.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR014395 Pen/GL7ACA/AHL_acylase
IPR023343 Penicillin_amidase_dom1
IPR002692 S45

The PANTHER Classification System

More...
PANTHERi
PTHR34218 PTHR34218, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01804 Penicil_amidase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001227 Pen_acylase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56235 SSF56235, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9L5D6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRVLHRAAS ALVMATVIGL APGVAFALAE 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 QVRPFERRQA
310 320 330 340 350
SYRLRQADGS TVDKPLEIRS SVHGPVFERA DGTAVAVRVA GLDRPGMLEQ
360 370 380 390 400
YFDMITAHSF DDYEAAMARM QVPTFNIVYA DREGTINYSF NGVAPKRAEG
410 420 430 440 450
DIAFWQGNVP GDSSRYLWTE THPLDDLPRV TNPPGGFVQN SNDPPWTPTW
460 470 480 490 500
PVTYTPRDHP SYLAPQTPHS LRAQQSVRLM SENDDLTLER FMALQFSHRA
510 520 530 540 550
VMADRTLPDL IPAALIDPDP EVQAAARLLA AWDREFTSDS RAALLFEEWA
560 570 580 590 600
RLFAGQNFAG QAAFATPWSL DKPVSTPYGV RDPKAAVDQL RTAIANTKRK
610 620 630 640 650
YGAIDRPFGD ASRMILNDVN VPGAAGYGNL GSFRVFTWSD PDENGIRTPV
660 670 680 690 700
HGETWVAMIE FSTPVRAYGL MSYGNSRQPG TTHYSDQIER VSRADFRELL
710 720
LRREQVEAAV QERTPFNFKP
Length:720
Mass (Da):79,779
Last modified:October 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAD624797845CC39B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF251710 Genomic DNA Translation: AAF64242.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAF64242

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF251710 Genomic DNA Translation: AAF64242.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FM2X-ray2.00A30-198[»]
B199-718[»]
1JVZX-ray2.60A30-187[»]
B199-718[»]
1JW0X-ray2.50A30-187[»]
B199-718[»]
1KEHX-ray2.50A30-718[»]
ProteinModelPortaliQ9L5D6
SMRiQ9L5D6
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS45.002

Proteomic databases

PRIDEiQ9L5D6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAF64242

Phylogenomic databases

KOiK12748

Enzyme and pathway databases

BRENDAi3.5.1.93 982

Miscellaneous databases

EvolutionaryTraceiQ9L5D6

Family and domain databases

Gene3Di1.10.439.10, 1 hit
3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR014395 Pen/GL7ACA/AHL_acylase
IPR023343 Penicillin_amidase_dom1
IPR002692 S45
PANTHERiPTHR34218 PTHR34218, 1 hit
PfamiView protein in Pfam
PF01804 Penicil_amidase, 1 hit
PIRSFiPIRSF001227 Pen_acylase, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiG7AC_BREDI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9L5D6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 1, 2000
Last modified: December 5, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again