AGUA_PSEFS
ID AGUA_PSEFS Reviewed; 368 AA.
AC C3K5U8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=PFLU_0293;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY46571.1; -; Genomic_DNA.
DR RefSeq; WP_012721716.1; NC_012660.1.
DR AlphaFoldDB; C3K5U8; -.
DR SMR; C3K5U8; -.
DR STRING; 294.SRM1_00342; -.
DR PRIDE; C3K5U8; -.
DR EnsemblBacteria; CAY46571; CAY46571; PFLU_0293.
DR KEGG; pfs:PFLU_0293; -.
DR PATRIC; fig|216595.4.peg.527; -.
DR eggNOG; COG2957; Bacteria.
DR HOGENOM; CLU_037682_1_0_6; -.
DR OMA; WCRDHGP; -.
DR OrthoDB; 771174at2; -.
DR UniPathway; UPA00534; UER00285.
DR Proteomes; UP000002332; 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_1000216094"
FT ACT_SITE 357
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ SEQUENCE 368 AA; 40397 MW; 9329248850F732DC CRC64;
MTTLHSTPRA DGFHMPAEWA PQTQTWMIWP ERPDNWRLGG KPAQAAHVAV AKAIARFEPV
TVAVSAGQYE NARARLDVPN IRVVEMSSDD AWVRDTGPTF VINRSGEVRG VNWDFNAWGG
FDGGLYSPWN RDSQIGGKIL EIERAPRYCT EGFVLEGGSI HVDGEGTLIT TEECLLNSNR
NPHLDRAQIE AVLSANLAVD KIIWLPDGLF NDETDGHVDN FCCYVRPGEV LLAWTDDPQD
PNYARCHAAM NVLQSSTDAQ GRSFTVHKMP IPGPLYATEA ECAGVDPVDG TQERNPTVRL
AGSYVNFLIV NGGIIAPSFD DPLDSQAKAI LQDLFPQHEV VMVPGRELLL GGGNIHCLTQ
QQPAPHKN