AGUA_PSESM
ID AGUA_PSESM Reviewed; 368 AA.
AC Q87UB2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=PSPTO_5393;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO58815.1; -; Genomic_DNA.
DR RefSeq; NP_795120.1; NC_004578.1.
DR RefSeq; WP_011105465.1; NC_004578.1.
DR AlphaFoldDB; Q87UB2; -.
DR SMR; Q87UB2; -.
DR STRING; 223283.PSPTO_5393; -.
DR EnsemblBacteria; AAO58815; AAO58815; PSPTO_5393.
DR GeneID; 1187080; -.
DR KEGG; pst:PSPTO_5393; -.
DR PATRIC; fig|223283.9.peg.5519; -.
DR eggNOG; COG2957; Bacteria.
DR HOGENOM; CLU_037682_1_0_6; -.
DR OMA; WCRDHGP; -.
DR OrthoDB; 771174at2; -.
DR PhylomeDB; Q87UB2; -.
DR UniPathway; UPA00534; UER00285.
DR Proteomes; UP000002515; 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_0000194339"
FT ACT_SITE 357
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ SEQUENCE 368 AA; 40863 MW; D132BF8ABDC95552 CRC64;
MTTLNSTPRA DGFHMPAEWA PQTQVWMVWP ERPDNWRLGG KPAQAAHVAI AKAIARFEPV
TVAVSAAQYD NARARLDMPN IRVVEMSSND AWVRDSGPTF VINDRGELRG VNWEFNAWGG
FDGGLYAPWN LDSQVGSKVL EIERCPRYAT QGFVLEGGSI HVDGEGTLIT TEECLLNRNR
NPHLTREQIE AVLSDYLAVD KIIWLPDGLF NDETDGHVDN FCCYIRPGEV LLAWTDDPED
PNYPRCHAAL SILENTRDAQ GRAFIVHKMP IPGPLFATEE ECAGVDQVHG SQERNPSVRL
AGSYVNFLIV NGGIIAPSFD DPMDEKAREI LQKLFPEHEV VMAPGRELLL GGGNIHCLTQ
QQPAPFKA