ID   AGUA_PSE14              Reviewed;         368 AA.
AC   Q48Q55;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=PSPPH_0153;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ33821.1; -; Genomic_DNA.
DR   RefSeq; WP_011167359.1; NC_005773.3.
DR   AlphaFoldDB; Q48Q55; -.
DR   SMR; Q48Q55; -.
DR   STRING; 264730.PSPPH_0153; -.
DR   EnsemblBacteria; AAZ33821; AAZ33821; PSPPH_0153.
DR   KEGG; psp:PSPPH_0153; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   OrthoDB; 771174at2; -.
DR   UniPathway; UPA00534; UER00285.
DR   Proteomes; UP000000551; 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.
FT   CHAIN           1..368
FT                   /note="Agmatine deiminase"
FT                   /id="PRO_1000070559"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   368 AA;  40709 MW;  2C8B49B941256F0F CRC64;
     MTTLNSTPRA DGFHMPAEWA PQTQVWMVWP ERPDNWRLGG KPAQAAHVAI AKAIARFEPV
     TVAVSAAQYD NARARLDVPN IRVVEMSSND AWVRDSGPTF VINERGEVRG VNWEFNAWGG
     FDGGLYAPWN LDSQLGSKVL EIERCPRYVT KGFVLEGGSI HVDGEGTLIT TEECLLNRNR
     NPHLTREQIE AILGDYLAVD KVVWLPDGLF NDETDGHVDN FCCYIRPGEV LLAWTDDPED
     PNYSRCHAAL GILENTLDAK GRAFIVHKMP IPGPLFATEE ECAGVDQVHG SQERNPSVRL
     AGSYVNFLIV NGGIIAPSFD DPMDEKAREL LQTLFPEHEV VMAPGRELLL GGGNIHCLTQ
     QQPAPHKA