ID   AGUA_PSEP1              Reviewed;         368 AA.
AC   A5VX45;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Pput_0281;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000712; ABQ76455.1; -; Genomic_DNA.
DR   RefSeq; WP_011953220.1; NC_009512.1.
DR   AlphaFoldDB; A5VX45; -.
DR   SMR; A5VX45; -.
DR   STRING; 351746.Pput_0281; -.
DR   EnsemblBacteria; ABQ76455; ABQ76455; Pput_0281.
DR   KEGG; ppf:Pput_0281; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   OrthoDB; 771174at2; -.
DR   UniPathway; UPA00534; UER00285.
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.
FT   CHAIN           1..368
FT                   /note="Agmatine deiminase"
FT                   /id="PRO_1000070564"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   368 AA;  40767 MW;  AD34BFE4A24E34C9 CRC64;
     MKTLNSTPRA DGFHMPAEWA PQTQVWMVWP ERPDNWRLGG KPAQAAHVTL AKAIARFEPV
     TVAASAGQYE NARRQLDQPN IRVVEISNDD AWVRDTGPTF VINGHGEVRG VDWGFNAWGG
     FDGGLYAPWN RDEELAAKVL EMERCQRYQT EGFVLEGGSI HVDGEGTVIT TEECLLNRNR
     NPHLSREQIE AVLRDHLAVD TVVWLPDGLY NDETDGHVDN FCCYVRPGEV LLAWTDDSND
     PNYARCHAAM DVLKNTRDAK GREFIVHKMP IPGPLYATAE ECAGVDQVAG SQERDPSVRL
     AGSYVNFLIV NGGIIAPSFD DPADAEARAI LARIFPDHEV VMIPGRELLL GGGNIHCLTQ
     QQPAPVKR