AGUA_PSEMY
ID AGUA_PSEMY Reviewed; 368 AA.
AC A4XP44;
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=Pmen_0337;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP83110.1; -; Genomic_DNA.
DR RefSeq; WP_011920610.1; NC_009439.1.
DR AlphaFoldDB; A4XP44; -.
DR SMR; A4XP44; -.
DR STRING; 399739.Pmen_0337; -.
DR PRIDE; A4XP44; -.
DR EnsemblBacteria; ABP83110; ABP83110; Pmen_0337.
DR KEGG; pmy:Pmen_0337; -.
DR PATRIC; fig|399739.8.peg.345; -.
DR eggNOG; COG2957; Bacteria.
DR HOGENOM; CLU_037682_1_0_6; -.
DR OMA; WCRDHGP; -.
DR OrthoDB; 771174at2; -.
DR UniPathway; UPA00534; UER00285.
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_1000070563"
FT ACT_SITE 357
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ SEQUENCE 368 AA; 40887 MW; F557B7635CDAB471 CRC64;
MTTLTTTPRA DGFHMPAEWA PHSQTWMVWP ERPDNWRNGG KPAQAAFTAV AKAIAQFEPV
TVCVSAAQYE NARARLDDDN IRLVEITTDD AWVRDTGPTF VINGRGEVRG VDWTFNAWGG
FDGGLYWPWQ RDDQVARKIL DIEGCKRYRT EGFVLEGGSI HVDGEGTLIT TEECLLNRNR
NPHLSREEIE AVLREHLAID TVIWLPEGLY NDETDGHVDN FCCYVRPGEV LLAWTDDQND
PNYPRCQAAM RVLESVRDAK GRQLIVHKMP IPGPIHASEE ECAGVDAAEG SQERSPAVRL
AGSYVNFLIV NGGIVAPSFD DPKDAEARAI LQQVFPEHRV VMVPGREILL GGGNIHCITQ
QQPAPQGA