G7AC_PSEU7
ID G7AC_PSEU7 Reviewed; 720 AA.
AC P07662; Q84I62;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 109.
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=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 Pseudomonas sp. (strain SY-77).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=269086;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12230561; DOI=10.1046/j.1432-1033.2002.03143.x;
RA Sio C.F., Riemens A.M., Van Der Laan J.M., Verhaert R.M., Quax W.J.;
RT "Directed evolution of a glutaryl acylase into an adipyl acylase.";
RL Eur. J. Biochem. 269:4495-4504(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-311, PROTEIN SEQUENCE OF 30-46 AND
RP 199-215, FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=2993240; DOI=10.1128/jb.163.3.1222-1228.1985;
RA Matsuda A., Komatsu K.;
RT "Molecular cloning and structure of the gene for 7 beta-(4-
RT carboxybutanamido)cephalosporanic acid acylase from a Pseudomonas strain.";
RL J. Bacteriol. 163:1222-1228(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-189 AND 199-720 OF WILD-TYPE
RP AND 30-720 OF MUTANT ALA-199, SUBUNIT, MUTAGENESIS OF SER-199, AND
RP AUTOCATALYTIC PROCESSING MECHANISM.
RX PubMed=12680762; DOI=10.1021/bi027181x;
RA Kim J.K., Yang I.S., Rhee S., Dauter Z., Lee Y.S., Park S.S., Kim K.H.;
RT "Crystal structures of glutaryl 7-aminocephalosporanic acid acylase:
RT insight into autoproteolytic activation.";
RL Biochemistry 42:4084-4093(2003).
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).
CC {ECO:0000269|PubMed:2993240}.
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: Heterotetramer of two alpha and two beta subunits processed
CC from the same precursor. {ECO:0000269|PubMed:12680762}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2993240}.
CC -!- INDUCTION: By glutaric acid. {ECO:0000269|PubMed:2993240}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR EMBL; AF458663; AAN39264.1; -; Genomic_DNA.
DR EMBL; M11436; AAA25826.1; -; Genomic_DNA.
DR PIR; A24928; A24928.
DR PDB; 1GK0; X-ray; 2.50 A; A/C=36-188, B/D=199-720.
DR PDB; 1GK1; X-ray; 2.40 A; A/C=36-188, B/D=199-720.
DR PDB; 1OR0; X-ray; 2.00 A; A/C=30-189, B/D=199-720.
DR PDB; 2ADV; X-ray; 2.24 A; A=30-195, B=199-226, C=227-720.
DR PDB; 2AE3; X-ray; 2.40 A; A=30-195, B=199-720.
DR PDB; 2AE4; X-ray; 2.30 A; A=30-195, B=199-720.
DR PDB; 2AE5; X-ray; 2.24 A; A=30-195, B=200-720.
DR PDB; 3S8R; X-ray; 2.50 A; A/B=30-720.
DR PDBsum; 1GK0; -.
DR PDBsum; 1GK1; -.
DR PDBsum; 1OR0; -.
DR PDBsum; 2ADV; -.
DR PDBsum; 2AE3; -.
DR PDBsum; 2AE4; -.
DR PDBsum; 2AE5; -.
DR PDBsum; 3S8R; -.
DR AlphaFoldDB; P07662; -.
DR SMR; P07662; -.
DR MEROPS; S45.002; -.
DR PRIDE; P07662; -.
DR BRENDA; 3.5.1.93; 5085.
DR EvolutionaryTrace; P07662; -.
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; Direct protein sequencing; Hydrolase;
KW Periplasm; Signal; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2993240"
FT CHAIN 30..720
FT /note="Glutaryl-7-aminocephalosporanic-acid acylase"
FT /id="PRO_0000027353"
FT CHAIN 30..189
FT /note="Glutaryl-7-aminocephalosporanic-acid acylase subunit
FT alpha"
FT /id="PRO_0000027354"
FT PROPEP 190..198
FT /note="Spacer peptide"
FT /evidence="ECO:0000269|PubMed:2993240"
FT /id="PRO_0000253351"
FT CHAIN 199..720
FT /note="Glutaryl-7-aminocephalosporanic-acid acylase subunit
FT beta"
FT /id="PRO_0000027355"
FT ACT_SITE 199
FT /note="Nucleophile"
FT ACT_SITE 221
FT /evidence="ECO:0000255"
FT ACT_SITE 653
FT /evidence="ECO:0000255"
FT MUTAGEN 199
FT /note="S->A: Loss of activity. Lack of autoprocessing."
FT /evidence="ECO:0000269|PubMed:12680762"
FT CONFLICT 79
FT /note="H -> Q (in Ref. 2; AAA25826)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="E -> D (in Ref. 2; AAA25826)"
FT /evidence="ECO:0000305"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 64..90
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:1OR0"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3S8R"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 347..355
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:2AE5"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 471..481
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 501..514
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 520..531
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 543..553
FT /evidence="ECO:0007829|PDB:1OR0"
FT TURN 555..558
FT /evidence="ECO:0007829|PDB:2ADV"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:1OR0"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 583..601
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 612..616
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 655..660
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 688..691
FT /evidence="ECO:0007829|PDB:1OR0"
FT TURN 692..694
FT /evidence="ECO:0007829|PDB:1OR0"
FT HELIX 703..709
FT /evidence="ECO:0007829|PDB:1OR0"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:1OR0"
SQ SEQUENCE 720 AA; 79627 MW; 643250675A266C33 CRC64;
MLRVLHRAAS ALVMATVIGL APAVAFALAE 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 QVRPFERPQA
SYRLRQADGT TVDKPLEIRS SVHGPVFERA DGTAVAVRVA GLDRPGMLEQ YFDMITADSF
DDYEAALARM QVPTFNIVYA DREGTINYSF NGVAPKRAEG DIAFWQGLVP GDSSRYLWTE
THPLDDLPRV TNPPGGFVQN SNDPPWTPTW PVTYTPKDFP SYLAPQTPHS LRAQQSVRLM
SENDDLTLER FMALQLSHRA VMADRTLPDL IPAALIDPDP EVQAAARLLA AWDREFTSDS
RAALLFEEWA RLFAGQNFAG QAGFATPWSL DKPVSTPYGV RDPKAAVDQL RTAIANTKRK
YGAIDRPFGD ASRMILNDVN VPGAAGYGNL GSFRVFTWSD PDENGVRTPV HGETWVAMIE
FSTPVRAYGL MSYGNSRQPG TTHYSDQIER VSRADFRELL LRREQVEAAV QERTPFNFKP
