GPUA_PSEAE
ID GPUA_PSEAE Reviewed; 318 AA.
AC Q9I6K2;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Guanidinopropionase;
DE EC=3.5.3.17 {ECO:0000269|PubMed:21600989};
GN Name=gpuA; OrderedLocusNames=PA0288;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH MANGANESE, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF TYR-157.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21600989; DOI=10.1016/j.jsb.2011.05.002;
RA Lee S.J., Kim D.J., Kim H.S., Lee B.I., Yoon H.J., Yoon J.Y., Kim K.H.,
RA Jang J.Y., Im H.N., An D.R., Song J.S., Kim H.J., Suh S.W.;
RT "Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and
RT guanidinopropionase, members of the ureohydrolase superfamily.";
RL J. Struct. Biol. 175:329-338(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of 3-guanidinopropanoate to beta-
CC alanine and urea. Possesses low activity against 4-guanidinobutanoate.
CC Has no activity against arginine and agmatine.
CC {ECO:0000269|PubMed:21600989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-guanidinopropanoate + H2O = beta-alanine + urea;
CC Xref=Rhea:RHEA:16029, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:57593, ChEBI:CHEBI:57966; EC=3.5.3.17;
CC Evidence={ECO:0000269|PubMed:21600989};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742,
CC ECO:0000269|PubMed:21600989};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742, ECO:0000269|PubMed:21600989};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.8 mM for 3-guanidinopropanoate {ECO:0000269|PubMed:21600989};
CC KM=37.3 mM for 4-guanidinobutanoate {ECO:0000269|PubMed:21600989};
CC Note=kcat is 106 sec(-1) with 3-guanidinopropanoate as substrate.
CC kcat is 57.6 sec(-1) for 4-guanidinobutanoate as substrate.;
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:21600989}.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00742}.
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DR EMBL; AE004091; AAG03677.1; -; Genomic_DNA.
DR PIR; H83610; H83610.
DR RefSeq; NP_248979.1; NC_002516.2.
DR RefSeq; WP_003112934.1; NZ_QZGE01000035.1.
DR PDB; 3NIP; X-ray; 2.50 A; A/B/C/D/E/F=1-318.
DR PDB; 3NIQ; X-ray; 2.07 A; A/B=1-318.
DR PDBsum; 3NIP; -.
DR PDBsum; 3NIQ; -.
DR AlphaFoldDB; Q9I6K2; -.
DR SMR; Q9I6K2; -.
DR STRING; 287.DR97_3250; -.
DR PaxDb; Q9I6K2; -.
DR EnsemblBacteria; AAG03677; AAG03677; PA0288.
DR GeneID; 880781; -.
DR KEGG; pae:PA0288; -.
DR PATRIC; fig|208964.12.peg.302; -.
DR PseudoCAP; PA0288; -.
DR HOGENOM; CLU_039478_0_0_6; -.
DR InParanoid; Q9I6K2; -.
DR OMA; HYAGVNH; -.
DR PhylomeDB; Q9I6K2; -.
DR BioCyc; PAER208964:G1FZ6-290-MON; -.
DR BRENDA; 3.5.3.17; 5087.
DR EvolutionaryTrace; Q9I6K2; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR GO; GO:0047972; F:guanidinopropionase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IBA:GO_Central.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01230; agmatinase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..318
FT /note="Guanidinopropionase"
FT /id="PRO_0000429142"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:21600989"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:21600989"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:21600989"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:21600989"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:21600989"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:21600989"
FT MUTAGEN 157
FT /note="Y->M: Reduces substrate affinity 10-fold and
FT catalytic efficiency 3-fold."
FT /evidence="ECO:0000269|PubMed:21600989"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3NIP"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3NIQ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3NIQ"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 178..188
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3NIP"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 211..230
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3NIQ"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:3NIQ"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:3NIQ"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3NIQ"
FT HELIX 294..317
FT /evidence="ECO:0007829|PDB:3NIQ"
SQ SEQUENCE 318 AA; 34189 MW; 5617D78C4AD626C3 CRC64;
MSNDHPQPLD AAEIPRFAGI PTFMRLPAFT DPAALQVGLI GVPWDGGTTN RAGARHGPRE
VRNLSSLMRK VHHVSRIAPY DLVRVGDLGD APVNPIDLLD SLRRIEGFYR QVHAAGTLPL
SVGGDHLVTL PIFRALGRER PLGMVHFDAH SDTNDRYFGD NPYTHGTPFR RAIEEGLLDP
LRTVQIGIRG SVYSPDDDAF ARECGIRVIH MEEFVELGVE ATLAEARRVV GAGPTYVSFD
VDVLDPAFAP GTGTPEIGGM TSLQAQQLVR GLRGLDLVGA DVVEVSPPFD VGGATALVGA
TMMFELLCLL AESAARSA
