(data stored in ACNUC7421 zone)

SWISSPROT: AGUA_PSEAB

ID   AGUA_PSEAB              Reviewed;         368 AA.
AC   Q02UC5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 62.
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};
GN   OrderedLocusNames=PA14_03810;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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: Agmatine + H(2)O = N-carbamoylputrescine +
CC       NH(3). {ECO:0000255|HAMAP-Rule:MF_01841}.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis
CC       via agmatine pathway; N-carbamoylputrescine from agmatine: step
CC       1/1. {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}.
DR   EMBL; CP000438; ABJ15255.1; -; Genomic_DNA.
DR   RefSeq; WP_003121701.1; NC_008463.1.
DR   ProteinModelPortal; Q02UC5; -.
DR   SMR; Q02UC5; -.
DR   EnsemblBacteria; ABJ15255; ABJ15255; PA14_03810.
DR   KEGG; pau:PA14_03810; -.
DR   HOGENOM; HOG000239346; -.
DR   KO; K10536; -.
DR   OMA; KQHGSLH; -.
DR   UniPathway; UPA00534; UER00285.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0047632; F:agmatine deiminase activity; IEA:UniProtKB-EC.
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   Pfam; PF04371; PAD_porph; 1.
DR   TIGRFAMs; TIGR03380; agmatine_aguA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02UC5.
DR   SWISS-2DPAGE; Q02UC5.
KW   Complete proteome; Hydrolase; Polyamine biosynthesis.
FT   CHAIN         1    368       Agmatine deiminase.
FT                                /FTId=PRO_1000070561.
FT   ACT_SITE    357    357       Amidino-cysteine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01841}.
SQ   SEQUENCE   368 AA;  41219 MW;  C5D6ACB125B89EA7 CRC64;
     MSNPTSTPRA DGFRMPAEWE PHEQTWMVWP ERPDNWRNGG KPAQAAFAAV AKAIARFEPV
     TVCASAGQYE NARARLDDGN IRVVEISSDD AWVRDTGPTF VIDDKGDVRG VDWGFNAWGG
     FEGGLYFPWQ RDDQVARKIL EIERRARYRT DDFVLEGGSI HVDGEGTLIT TEECLLNHNR
     NPHLSQVEIE RTLRDYLAVD SIIWLPNGLY NDETDGHVDN FCCYVRPGEV LLAWTDDQDD
     PNYLRCQAAL RVLEESRDAK GRKLVVHKMP IPGPLYATQE ECDGVDIVEG SQPRDPSIRL
     AGSYVNFLIV NGGIVAPSFD DPKDAEARAI LQRVFPEHEV VMVPGREILL GGGNIHCITQ
     QQPAPRKA
//

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