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Protein

Glutaryl-7-aminocephalosporanic-acid acylase

Gene
N/A
Organism
Brevundimonas diminuta (Pseudomonas diminuta)
Status
Reviewed-Annotation score: Annotation score: 4 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). Can not efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as substrates.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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

BRENDAi3.5.1.93. 982.

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
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
OrganismiBrevundimonas diminuta (Pseudomonas diminuta)
Taxonomic identifieri293 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeBrevundimonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929By similarityAdd
BLAST
Chaini30 – 720691Glutaryl-7-aminocephalosporanic-acid acylasePRO_0000027356Add
BLAST
Chaini30 – 187158Glutaryl-7-aminocephalosporanic-acid acylase subunit alphaPRO_0000253782Add
BLAST
Propeptidei188 – 19811Spacer peptidePRO_0000253783Add
BLAST
Chaini199 – 720522Glutaryl-7-aminocephalosporanic-acid acylase subunit betaPRO_0000253784Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

Heterodimer of a small subunit and a large subunit 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 – 17513Combined sources
Turni176 – 1794Combined sources
Helixi182 – 1865Combined 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 strandi296 – 30510Combined sources
Beta strandi311 – 32010Combined sources
Beta strandi322 – 3287Combined sources
Beta strandi334 – 3396Combined sources
Turni340 – 3434Combined 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 – 51515Combined sources
Helixi520 – 53011Combined sources
Helixi543 – 55311Combined 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
1FM2X-ray2.00A30-198[»]
B199-718[»]
1JVZX-ray2.60A30-187[»]
B199-718[»]
1JW0X-ray2.50A30-187[»]
B199-718[»]
1KEHX-ray2.50A30-718[»]
ProteinModelPortaliQ9L5D6.
SMRiQ9L5D6. Positions 36-718.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9L5D6.

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.
IPR002692. Pen/cephal_acylase.
IPR023343. Penicillin_amidase_dom1.
[Graphical view]
PfamiPF01804. Penicil_amidase. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

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
Checksum:iAD624797845CC39B
GO

Sequence databases

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

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:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 36-718.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS45.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 2 hits.
InterProiIPR029055. Ntn_hydrolases_N.
IPR002692. Pen/cephal_acylase.
IPR023343. Penicillin_amidase_dom1.
[Graphical view]
PfamiPF01804. Penicil_amidase. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and the nucleotide sequence of a Pseudomonas diminuta KAC-1 glutaryl 7-aminocephalosporanic acid acylase gene."
    Kim D.-W., Kang S.-M., Yoon K.-H.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KAC-1.
  2. "Isolation of novel Pseudomonas diminuta KAC-1 strain producing glutaryl 7-aminocephalosporanic acid acylase."
    Kim D.-W., Yoon K.-H.
    J. Microbiol. 37:200-205(1999)
    Cited for: FUNCTION.
    Strain: KAC-1.
  3. "The 2.0 A crystal structure of cephalosporin acylase."
    Kim Y., Yoon K.-H., Khang Y., Turley S., Hol W.G.J.
    Structure 8:1059-1068(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-720, SUBUNIT.
    Strain: KAC-1.
  4. "Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity."
    Kim Y., Hol W.G.J.
    Chem. Biol. 8:1253-1264(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-187 AND 199-720 IN COMPLEXES WITH SUBSTRATE AND GLUTARATE, REACTION MECHANISM.
    Strain: KAC-1.
  5. "Precursor structure of cephalosporin acylase. Insights into autoproteolytic activation in a new N-terminal hydrolase family."
    Kim Y., Kim S., Earnest T.N., Hol W.G.J.
    J. Biol. Chem. 277:2823-2829(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-720 OF MUTANT ALA-199, IDENTIFICATION BY MASS SPECTROMETRY, AUTOCATALYTIC CLEAVAGE POSITIONS.
    Strain: KAC-1.

Entry informationi

Entry nameiG7AC_BREDI
AccessioniPrimary (citable) accession number: Q9L5D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 1, 2000
Last modified: October 14, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.