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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
 
 
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