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-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). Cannot 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)DescriptionActionsGraphical viewLength
Active sitei199Nucleophile1
Active sitei221Sequence analysis1
Active sitei653Sequence analysis1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29By similarityAdd BLAST29
ChainiPRO_000002735630 – 720Glutaryl-7-aminocephalosporanic-acid acylaseAdd BLAST691
ChainiPRO_000025378230 – 187Glutaryl-7-aminocephalosporanic-acid acylase subunit alphaAdd BLAST158
PropeptideiPRO_0000253783188 – 198Spacer peptideAdd BLAST11
ChainiPRO_0000253784199 – 720Glutaryl-7-aminocephalosporanic-acid acylase subunit betaAdd BLAST522

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

1720
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 52Combined sources5
Beta strandi57 – 60Combined sources4
Helixi64 – 90Combined sources27
Helixi94 – 98Combined sources5
Helixi100 – 102Combined sources3
Helixi103 – 111Combined sources9
Helixi114 – 123Combined sources10
Helixi127 – 146Combined sources20
Helixi148 – 150Combined sources3
Helixi153 – 158Combined sources6
Helixi163 – 175Combined sources13
Turni176 – 179Combined sources4
Helixi182 – 186Combined sources5
Beta strandi200 – 204Combined sources5
Helixi206 – 208Combined sources3
Beta strandi209 – 212Combined sources4
Beta strandi215 – 219Combined sources5
Beta strandi221 – 225Combined sources5
Helixi227 – 229Combined sources3
Beta strandi231 – 237Combined sources7
Beta strandi242 – 248Combined sources7
Beta strandi255 – 258Combined sources4
Beta strandi260 – 267Combined sources8
Beta strandi274 – 278Combined sources5
Beta strandi285 – 288Combined sources4
Beta strandi291 – 293Combined sources3
Beta strandi296 – 305Combined sources10
Beta strandi311 – 320Combined sources10
Beta strandi322 – 328Combined sources7
Beta strandi334 – 339Combined sources6
Turni340 – 343Combined sources4
Helixi347 – 355Combined sources9
Helixi360 – 367Combined sources8
Beta strandi376 – 381Combined sources6
Beta strandi386 – 390Combined sources5
Helixi402 – 406Combined sources5
Beta strandi407 – 412Combined sources6
Helixi414 – 416Combined sources3
Helixi424 – 426Combined sources3
Beta strandi429 – 432Combined sources4
Beta strandi436 – 439Combined sources4
Beta strandi441 – 443Combined sources3
Beta strandi448 – 451Combined sources4
Helixi456 – 458Combined sources3
Helixi471 – 481Combined sources11
Helixi488 – 495Combined sources8
Helixi501 – 515Combined sources15
Helixi520 – 530Combined sources11
Helixi543 – 553Combined sources11
Beta strandi564 – 566Combined sources3
Turni573 – 575Combined sources3
Beta strandi577 – 581Combined sources5
Helixi583 – 601Combined sources19
Beta strandi602 – 605Combined sources4
Helixi608 – 611Combined sources4
Beta strandi612 – 616Combined sources5
Beta strandi619 – 622Combined sources4
Helixi628 – 630Combined sources3
Beta strandi633 – 638Combined sources6
Beta strandi649 – 653Combined sources5
Beta strandi655 – 660Combined sources6
Beta strandi666 – 671Combined sources6
Beta strandi682 – 687Combined sources6
Helixi688 – 691Combined sources4
Turni692 – 694Combined sources3
Helixi703 – 709Combined sources7
Beta strandi710 – 715Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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...

Miscellaneous databases

EvolutionaryTraceiQ9L5D6.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S45 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK12748.

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.

Genome annotation databases

KEGGiag:AAF64242.

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
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.

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. 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...

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: November 2, 2016
This is version 73 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.