GBUA_PSEAE
ID GBUA_PSEAE Reviewed; 319 AA.
AC Q9I3S3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Guanidinobutyrase;
DE EC=3.5.3.7 {ECO:0000269|PubMed:12029055, ECO:0000269|PubMed:21600989};
GN Name=gbuA; OrderedLocusNames=PA1421;
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 PROTEIN SEQUENCE OF 1-9, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12029055; DOI=10.1128/jb.184.12.3377-3384.2002;
RA Nakada Y., Itoh Y.;
RT "Characterization and regulation of the gbuA gene, encoding
RT guanidinobutyrase in the arginine dehydrogenase pathway of Pseudomonas
RT aeruginosa PAO1.";
RL J. Bacteriol. 184:3377-3384(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MANGANESE, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF MET-161.
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 specifically the hydrolysis of 4-guanidinobutanoate
CC to 4-aminobutanoate and urea. Has no activity against arginine,
CC agmatine, 3-guanidinopropionate and guanidinoacetate.
CC {ECO:0000269|PubMed:12029055, ECO:0000269|PubMed:21600989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-guanidinobutanoate + H2O = 4-aminobutanoate + urea;
CC Xref=Rhea:RHEA:19501, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:57486, ChEBI:CHEBI:59888; EC=3.5.3.7;
CC Evidence={ECO:0000269|PubMed:12029055, 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:12029055, ECO:0000269|PubMed:21600989};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742, ECO:0000269|PubMed:12029055,
CC ECO:0000269|PubMed:21600989};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=49 mM for 4-guanidinobutanoate {ECO:0000269|PubMed:12029055};
CC KM=10.7 mM for 4-guanidinobutanoate {ECO:0000269|PubMed:21600989};
CC Note=kcat is 1012 sec(-1) (PubMed:12029055). kcat is 94.7 sec(-1)
CC (PubMed:21600989). {ECO:0000269|PubMed:12029055,
CC ECO:0000269|PubMed:21600989};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:12029055};
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; AAG04810.1; -; Genomic_DNA.
DR PIR; H83468; H83468.
DR RefSeq; NP_250112.1; NC_002516.2.
DR RefSeq; WP_003082966.1; NZ_QZGE01000005.1.
DR PDB; 3NIO; X-ray; 2.00 A; A/B/C/D/E/F=1-319.
DR PDBsum; 3NIO; -.
DR AlphaFoldDB; Q9I3S3; -.
DR SMR; Q9I3S3; -.
DR STRING; 287.DR97_602; -.
DR PaxDb; Q9I3S3; -.
DR PRIDE; Q9I3S3; -.
DR DNASU; 881747; -.
DR EnsemblBacteria; AAG04810; AAG04810; PA1421.
DR GeneID; 881747; -.
DR KEGG; pae:PA1421; -.
DR PATRIC; fig|208964.12.peg.1470; -.
DR PseudoCAP; PA1421; -.
DR HOGENOM; CLU_039478_0_0_6; -.
DR InParanoid; Q9I3S3; -.
DR OMA; CIDAGFV; -.
DR PhylomeDB; Q9I3S3; -.
DR BioCyc; MetaCyc:MON-11558; -.
DR BioCyc; PAER208964:G1FZ6-1447-MON; -.
DR BRENDA; 3.5.3.7; 5087.
DR SABIO-RK; Q9I3S3; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR GO; GO:0047971; F:guanidinobutyrase activity; IDA:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IDA:PseudoCAP.
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; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..319
FT /note="Guanidinobutyrase"
FT /id="PRO_0000429141"
FT BINDING 129
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 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 152
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 154
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 156
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 243
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 245
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 161
FT /note="M->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21600989"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3NIO"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3NIO"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3NIO"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3NIO"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:3NIO"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3NIO"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3NIO"
FT HELIX 297..311
FT /evidence="ECO:0007829|PDB:3NIO"
SQ SEQUENCE 319 AA; 34728 MW; E119C5DD35CE9089 CRC64;
MDKNLHQPLG GNEMPRFGGI ATMMRLPHVQ SPAELDALDA AFVGVPLDIG TSLRSGTRFG
PREIRAESVM IRPYNMATGA APFDSLNVAD IGDVAINTFN LLEAVRIIEQ EYDRILGHGI
LPLTLGGDHT ITLPILRAIK KKHGKVGLVH VDAHADVNDH MFGEKIAHGT TFRRAVEEDL
LDCDRVVQIG LRAQGYTAED FNWSRKQGFR VVQAEECWHK SLEPLMAEVR EKVGGGPVYL
SFDIDGIDPA WAPGTGTPEI GGLTTIQAME IIRGCQGLDL IGCDLVEVSP PYDTTGNTSL
LGANLLYEML CVLPGVVRR
