AGUA_PSEU2
ID AGUA_PSEU2 Reviewed; 368 AA.
AC Q4ZLL3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Psyr_4932;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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; CP000075; AAY39959.1; -; Genomic_DNA.
DR RefSeq; WP_011269318.1; NC_007005.1.
DR RefSeq; YP_237997.1; NC_007005.1.
DR AlphaFoldDB; Q4ZLL3; -.
DR SMR; Q4ZLL3; -.
DR STRING; 205918.Psyr_4932; -.
DR EnsemblBacteria; AAY39959; AAY39959; Psyr_4932.
DR KEGG; psb:Psyr_4932; -.
DR PATRIC; fig|205918.7.peg.5096; -.
DR eggNOG; COG2957; Bacteria.
DR HOGENOM; CLU_037682_1_0_6; -.
DR OMA; WCRDHGP; -.
DR UniPathway; UPA00534; UER00285.
DR Proteomes; UP000000426; 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_1000070565"
FT ACT_SITE 357
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ SEQUENCE 368 AA; 40856 MW; 54D68C772B6154C0 CRC64;
MTTLNSTPRA DGFHMPAEWA PQTQVWMVWP ERPDNWRLGG KPAQAAHVAI AKAIARFEPV
TVAVSAAQYD NARARLDMPN IRVVEMSSND AWVRDSGPTF VINDRGEVRG VNWEFNAWGG
FDGGLYAPWN LDSQLGGKVL EIERCPRYVT EGFVLEGGSI HVDGEGTLIT TEECLLNRNR
NPHLTREQIE TILGDYLAVD KVIWLPEGLF NDETDGHVDN FCCYIRPGEV LLAWTDDPED
PNYSRCHAAL SILENTLDAK GRAFIVHKMP IPGPLFATEE ECAGVDQVHG SQERNPSVRL
AGSYVNFLIV NGGIIAPSFD DPMDEKAREI LQKLFPEHEV VMAPGRELLL GGGNIHCLTQ
QQPAPHKN
