ID   AGUA_PSEU5              Reviewed;         368 AA.
AC   A4VFL7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=PST_0060;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000304; ABP77768.1; -; Genomic_DNA.
DR   RefSeq; WP_011911310.1; NC_009434.1.
DR   AlphaFoldDB; A4VFL7; -.
DR   SMR; A4VFL7; -.
DR   STRING; 379731.PST_0060; -.
DR   EnsemblBacteria; ABP77768; ABP77768; PST_0060.
DR   KEGG; psa:PST_0060; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   UniPathway; UPA00534; UER00285.
DR   Proteomes; UP000000233; 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_1000070566"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   368 AA;  40655 MW;  5474B00D48AF52A2 CRC64;
     MTTLTSTPRQ DGYYMPAEWA PHSQTWMVWP QRPDNWRDNA APAQAAFAAV AKAIARFEPV
     TVCASAEQYL AARAALDDPR IRVVEMSSDD AWVRDTGPTF VIDDNGGLRG VDWTFNAWGG
     KDGGLYADWQ RDDEVARKIL EIEYCDRYRT EGFVLEGGSI HVDGEGTLIT TEECLLNRNR
     NPQLSREQIE AVLREHLAVD SIIWLPHGLF NDETDGHVDN FCCFVRPGEV LLAWTDDAND
     PNYARCQAAM AVLQRARDAK GRALIVHKIP IPGPLHASDA ECAGVVALDG SQLRDPSIRL
     AGSYVNFLIV NGGIIAPAFG DPLDGEAERI LREVFPEHDV VMVPGREILL GGGNIHCITQ
     QQPAPFVR