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AGUA_PSEAE
ID   AGUA_PSEAE              Reviewed;         368 AA.
AC   Q9I6J9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Agmatine deiminase;
DE            EC=3.5.3.12;
DE   AltName: Full=Agmatine iminohydrolase;
GN   Name=aguA; OrderedLocusNames=PA0292;
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   CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=11673419; DOI=10.1128/jb.183.22.6517-6524.2001;
RA   Nakada Y., Jiang Y., Nishijyo T., Itoh Y., Lu C.-D.;
RT   "Molecular characterization and regulation of the aguBA operon, responsible
RT   for agmatine utilization in Pseudomonas aeruginosa PAO1.";
RL   J. Bacteriol. 183:6517-6524(2001).
RN   [3]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=12634339; DOI=10.1099/mic.0.26009-0;
RA   Nakada Y., Itoh Y.;
RT   "Identification of the putrescine biosynthetic genes in Pseudomonas
RT   aeruginosa and characterization of agmatine deiminase and N-
RT   carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway.";
RL   Microbiology 149:707-714(2003).
CC   -!- FUNCTION: Mediates the hydrolysis of agmatine into N-
CC       carbamoylputrescine in the arginine decarboxylase (ADC) pathway of
CC       putrescine biosynthesis, a basic polyamine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=agmatine + H2O = N-carbamoylputrescine + NH4(+);
CC         Xref=Rhea:RHEA:18037, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58145, ChEBI:CHEBI:58318; EC=3.5.3.12;
CC         Evidence={ECO:0000269|PubMed:11673419};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.6 mM for agmatin {ECO:0000269|PubMed:12634339};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       agmatine pathway; N-carbamoylputrescine from agmatine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12634339}.
CC   -!- INDUCTION: By agmatine and N-carbamoylputrescine.
CC       {ECO:0000269|PubMed:11673419}.
CC   -!- SIMILARITY: Belongs to the agmatine deiminase family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG03681.1; -; Genomic_DNA.
DR   PIR; F83608; F83608.
DR   RefSeq; NP_248983.1; NC_002516.2.
DR   RefSeq; WP_003104504.1; NZ_QZGE01000035.1.
DR   AlphaFoldDB; Q9I6J9; -.
DR   SMR; Q9I6J9; -.
DR   STRING; 287.DR97_3254; -.
DR   PaxDb; Q9I6J9; -.
DR   PRIDE; Q9I6J9; -.
DR   EnsemblBacteria; AAG03681; AAG03681; PA0292.
DR   GeneID; 879730; -.
DR   KEGG; pae:PA0292; -.
DR   PATRIC; fig|208964.12.peg.306; -.
DR   PseudoCAP; PA0292; -.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   InParanoid; Q9I6J9; -.
DR   OMA; WCRDHGP; -.
DR   PhylomeDB; Q9I6J9; -.
DR   BioCyc; MetaCyc:MON-30; -.
DR   BioCyc; PAER208964:G1FZ6-294-MON; -.
DR   BRENDA; 3.5.3.12; 5087.
DR   UniPathway; UPA00534; UER00285.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0047632; F:agmatine deiminase activity; IDA:PseudoCAP.
DR   GO; GO:0004668; F:protein-arginine deiminase activity; IEA:InterPro.
DR   GO; GO:0033388; P:putrescine biosynthetic process from arginine; IMP:PseudoCAP.
DR   HAMAP; MF_01841; Agmatine_deimin; 1.
DR   InterPro; IPR017754; Agmatine_deiminase.
DR   InterPro; IPR007466; Peptidyl-Arg-deiminase_porph.
DR   PANTHER; PTHR31377; PTHR31377; 1.
DR   Pfam; PF04371; PAD_porph; 1.
DR   TIGRFAMs; TIGR03380; agmatine_aguA; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Polyamine biosynthesis; Reference proteome.
FT   CHAIN           1..368
FT                   /note="Agmatine deiminase"
FT                   /id="PRO_0000194337"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  41191 MW;  E805F3C907AC1E79 CRC64;
     MSNPTSTPRA DGFRMPAEWE PHEQTWMVWP ERPDNWRNGG KPAQAAFAAV AKAIARFEPV
     TVCASAGQYE NARARLDDGN IRVVEISSDD AWVRDTGPTF VIDDKGDVRG VDWGFNAWGG
     FEGGLYFPWQ RDDQVARKIL EIERRARYRT DDFVLEGGSI HVDGEGTLIT TEECLLNHNR
     NPHLSQAEIE RTLRDYLAVE SIIWLPNGLY NDETDGHVDN FCCYARPGEV LLAWTDDQDD
     PNYLRCQAAL RVLEESRDAK GRKLVVHKMP IPGPLYATQE ECDGVDIVEG SQPRDPSIRL
     AGSYVNFLIV NGGIIAPSFD DPKDAEARAI LQRVFPEHEV VMVPGREILL GGGNIHCITQ
     QQPAPRKA
 
 
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