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 03-MAY-2023, entry version 112. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 CDD; cd01936; Ntn_CA; 1. DR Gene3D; 1.10.1400.10; -; 1. DR Gene3D; 2.30.120.10; -; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1. DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1. DR Pfam; PF01804; Penicil_amidase; 1. DR PIRSF; PIRSF001227; Pen_acylase; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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 //