ID   AGUA_PSEPK              Reviewed;         368 AA.
AC   Q88R68;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Agmatine deiminase {ECO:0000255|HAMAP-Rule:MF_01841};
DE            EC=3.5.3.12 {ECO:0000255|HAMAP-Rule:MF_01841};
DE   AltName: Full=Agmatine iminohydrolase {ECO:0000255|HAMAP-Rule:MF_01841};
GN   Name=aguA {ECO:0000255|HAMAP-Rule:MF_01841}; OrderedLocusNames=PP_0266;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Mediates the hydrolysis of agmatine into N-
CC       carbamoylputrescine in the arginine decarboxylase (ADC) pathway of
CC       putrescine biosynthesis, a basic polyamine. {ECO:0000255|HAMAP-
CC       Rule:MF_01841}.
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:0000255|HAMAP-Rule:MF_01841};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       agmatine pathway; N-carbamoylputrescine from agmatine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01841}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01841}.
CC   -!- SIMILARITY: Belongs to the agmatine deiminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01841}.
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DR   EMBL; AE015451; AAN65897.1; -; Genomic_DNA.
DR   RefSeq; NP_742433.1; NC_002947.4.
DR   RefSeq; WP_010951636.1; NC_002947.4.
DR   AlphaFoldDB; Q88R68; -.
DR   SMR; Q88R68; -.
DR   STRING; 160488.PP_0266; -.
DR   EnsemblBacteria; AAN65897; AAN65897; PP_0266.
DR   KEGG; ppu:PP_0266; -.
DR   PATRIC; fig|160488.4.peg.284; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   PhylomeDB; Q88R68; -.
DR   BioCyc; PPUT160488:G1G01-288-MON; -.
DR   UniPathway; UPA00534; UER00285.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0047632; F:agmatine deiminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004668; F:protein-arginine deiminase activity; IEA:InterPro.
DR   GO; GO:0033388; P:putrescine biosynthetic process from arginine; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Hydrolase; Polyamine biosynthesis; Reference proteome.
FT   CHAIN           1..368
FT                   /note="Agmatine deiminase"
FT                   /id="PRO_0000194338"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   368 AA;  40837 MW;  486A81A9EC390CED CRC64;
     MKTLNSTPRA DGFHMPAEWA PQTQVWMVWP ERPDNWRLGG KPAQAAHVTL AKAIARFEPV
     TVAVSAGQYE NARRQLDQPN IRVVEISNDD AWVRDTGPTF VINDHGEVRG VDWGFNAWGG
     FDGGLYAPWN RDEELAAKVL EMERCQRYQT EGFVLEGGSI HVDGEGTVIT TEECLLNRNR
     NPHLSREQIE AVLRDHLAVD TVVWLPDGLY NDETDGHVDN FCCYVRPGEV LLAWTDDSND
     PNYARCHAAM DVLKNTRDAK GREFIVHKMP IPGPLFATAE ECAGVDQVAG SQERDPSVRL
     AGSYVNFLIV NGGIIAPSFD DPADAEARAI LARIFPDHEV VMIPGRELLL GGGNIHCLTQ
     QQPAPVKR