G7AC_BREDI
ID G7AC_BREDI Reviewed; 720 AA.
AC Q9L5D6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Glutaryl-7-aminocephalosporanic-acid acylase;
DE Short=Glutaryl-7-ACA acylase;
DE EC=3.5.1.93;
DE AltName: Full=7-beta-(4-carboxybutanamido)cephalosporanic acid acylase;
DE AltName: Full=CAD;
DE AltName: Full=GL-7-ACA acylase;
DE Short=GCA;
DE Contains:
DE RecName: Full=Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha;
DE Short=Glutaryl-7-ACA acylase subunit alpha;
DE Contains:
DE RecName: Full=Glutaryl-7-aminocephalosporanic-acid acylase subunit beta;
DE Short=Glutaryl-7-ACA acylase subunit beta;
DE Flags: Precursor;
OS Brevundimonas diminuta (Pseudomonas diminuta).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=293;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KAC-1;
RA Kim D.-W., Kang S.-M., Yoon K.-H.;
RT "Cloning and the nucleotide sequence of a Pseudomonas diminuta KAC-1
RT glutaryl 7-aminocephalosporanic acid acylase gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RC STRAIN=KAC-1;
RA Kim D.-W., Yoon K.-H.;
RT "Isolation of novel Pseudomonas diminuta KAC-1 strain producing glutaryl 7-
RT aminocephalosporanic acid acylase.";
RL J. Microbiol. 37:200-205(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-720, AND SUBUNIT.
RC STRAIN=KAC-1;
RX PubMed=11080627; DOI=10.1016/s0969-2126(00)00505-0;
RA Kim Y., Yoon K.-H., Khang Y., Turley S., Hol W.G.J.;
RT "The 2.0 A crystal structure of cephalosporin acylase.";
RL Structure 8:1059-1068(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-187 AND 199-720 IN COMPLEXES
RP WITH SUBSTRATE AND GLUTARATE, AND REACTION MECHANISM.
RC STRAIN=KAC-1;
RX PubMed=11755403; DOI=10.1016/s1074-5521(01)00092-8;
RA Kim Y., Hol W.G.J.;
RT "Structure of cephalosporin acylase in complex with glutaryl-7-
RT aminocephalosporanic acid and glutarate: insight into the basis of its
RT substrate specificity.";
RL Chem. Biol. 8:1253-1264(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-720 OF MUTANT ALA-199,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND AUTOCATALYTIC CLEAVAGE POSITIONS.
RC STRAIN=KAC-1;
RX PubMed=11706000; DOI=10.1074/jbc.m108888200;
RA Kim Y., Kim S., Earnest T.N., Hol W.G.J.;
RT "Precursor structure of cephalosporin acylase. Insights into
RT autoproteolytic activation in a new N-terminal hydrolase family.";
RL J. Biol. Chem. 277:2823-2829(2002).
CC -!- FUNCTION: Catalyzes the deacylation of 7 beta-(4-
CC carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic
CC acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). Cannot
CC efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as
CC substrates. {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-
CC aminocephalosporanate + glutarate; Xref=Rhea:RHEA:23508,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30921, ChEBI:CHEBI:58501,
CC ChEBI:CHEBI:58693; EC=3.5.1.93;
CC -!- SUBUNIT: Heterodimer of a small subunit and a large subunit processed
CC from the same precursor. {ECO:0000269|PubMed:11080627}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR EMBL; AF251710; AAF64242.1; -; Genomic_DNA.
DR PDB; 1FM2; X-ray; 2.00 A; A=30-198, B=199-718.
DR PDB; 1JVZ; X-ray; 2.60 A; A=30-187, B=199-718.
DR PDB; 1JW0; X-ray; 2.50 A; A=30-187, B=199-718.
DR PDB; 1KEH; X-ray; 2.50 A; A=30-718.
DR PDBsum; 1FM2; -.
DR PDBsum; 1JVZ; -.
DR PDBsum; 1JW0; -.
DR PDBsum; 1KEH; -.
DR AlphaFoldDB; Q9L5D6; -.
DR SMR; Q9L5D6; -.
DR MEROPS; S45.002; -.
DR KEGG; ag:AAF64242; -.
DR BRENDA; 3.5.1.93; 982.
DR EvolutionaryTrace; Q9L5D6; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0033968; F:glutaryl-7-aminocephalosporanic-acid acylase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 1.10.439.10; -; 1.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR InterPro; IPR043147; Penicillin_amidase_A-knob.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218; PTHR34218; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Hydrolase; Periplasm; Signal; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..720
FT /note="Glutaryl-7-aminocephalosporanic-acid acylase"
FT /id="PRO_0000027356"
FT CHAIN 30..187
FT /note="Glutaryl-7-aminocephalosporanic-acid acylase subunit
FT alpha"
FT /id="PRO_0000253782"
FT PROPEP 188..198
FT /note="Spacer peptide"
FT /id="PRO_0000253783"
FT CHAIN 199..720
FT /note="Glutaryl-7-aminocephalosporanic-acid acylase subunit
FT beta"
FT /id="PRO_0000253784"
FT ACT_SITE 199
FT /note="Nucleophile"
FT ACT_SITE 221
FT /evidence="ECO:0000255"
FT ACT_SITE 653
FT /evidence="ECO:0000255"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 64..90
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:1FM2"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:1FM2"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 347..355
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 471..481
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 501..515
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 520..530
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 543..553
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:1FM2"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 583..601
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:1JVZ"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 612..616
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 655..660
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 688..691
FT /evidence="ECO:0007829|PDB:1FM2"
FT TURN 692..694
FT /evidence="ECO:0007829|PDB:1FM2"
FT HELIX 703..709
FT /evidence="ECO:0007829|PDB:1FM2"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:1FM2"
SQ SEQUENCE 720 AA; 79779 MW; AD624797845CC39B CRC64;
MLRVLHRAAS ALVMATVIGL APGVAFALAE PTSTPQAPIA AYKPRSNEIL WDGYGVPHIY
GVDAPSAFYG YGWAQARSHG DNILRLYGEA RGKGAEYWGP DYEQTTVWLL TNGVPERAQQ
WYAQQSPDFR ANLDAFAAGI NAYAQQNPDD ISPEVRQVLP VSGADVVAHA HRLMNFLYVA
SPGRTLGEGD PPDLADQGSN SWAVAPGKTA NGNALLLQNP HLSWTTDYFT YYEAHLVTPD
FEIYGATQIG LPVIRFAFNQ RMGITNTVNG MVGATNYRLT LQDGGYLYDG QVRPFERRQA
SYRLRQADGS TVDKPLEIRS SVHGPVFERA DGTAVAVRVA GLDRPGMLEQ YFDMITAHSF
DDYEAAMARM QVPTFNIVYA DREGTINYSF NGVAPKRAEG DIAFWQGNVP GDSSRYLWTE
THPLDDLPRV TNPPGGFVQN SNDPPWTPTW PVTYTPRDHP SYLAPQTPHS LRAQQSVRLM
SENDDLTLER FMALQFSHRA VMADRTLPDL IPAALIDPDP EVQAAARLLA AWDREFTSDS
RAALLFEEWA RLFAGQNFAG QAAFATPWSL DKPVSTPYGV RDPKAAVDQL RTAIANTKRK
YGAIDRPFGD ASRMILNDVN VPGAAGYGNL GSFRVFTWSD PDENGIRTPV HGETWVAMIE
FSTPVRAYGL MSYGNSRQPG TTHYSDQIER VSRADFRELL LRREQVEAAV QERTPFNFKP
