(data stored in ACNUC9543 zone)

SWISSPROT: A0A0H2Y4X0_YERPA

ID   A0A0H2Y4X0_YERPA        Unreviewed;       371 AA.
AC   A0A0H2Y4X0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 17.
DE   RecName: Full=Putative agmatine deiminase {ECO:0000256|HAMAP-Rule:MF_01841};
DE            EC=3.5.3.12 {ECO:0000256|HAMAP-Rule:MF_01841};
DE   AltName: Full=Agmatine iminohydrolase {ECO:0000256|HAMAP-Rule:MF_01841};
GN   Name=aguA {ECO:0000256|HAMAP-Rule:MF_01841};
GN   OrderedLocusNames=YPA_0326 {ECO:0000313|EMBL:ABG12294.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12294.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12294.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12294.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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:0000256|HAMAP-Rule:MF_01841,
CC         ECO:0000256|SAAS:SAAS01119986};
CC   -!- SIMILARITY: Belongs to the agmatine deiminase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01841, ECO:0000256|SAAS:SAAS00963619}.
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DR   EMBL; CP000308; ABG12294.1; -; Genomic_DNA.
DR   RefSeq; WP_002209980.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12294; ABG12294; YPA_0326.
DR   KEGG; ypa:YPA_0326; -.
DR   KO; K10536; -.
DR   OMA; KQHGSLH; -.
DR   Proteomes; UP000001971; 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:0009446; P:putrescine biosynthetic process; IEA:InterPro.
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;
DR   PRODOM; A0A0H2Y4X0.
DR   SWISS-2DPAGE; A0A0H2Y4X0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01841,
KW   ECO:0000256|SAAS:SAAS00963620}.
FT   ACT_SITE    363    363       Amidino-cysteine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01841}.
SQ   SEQUENCE   371 AA;  41038 MW;  38587343D50EFD84 CRC64;
     MSVQDTMLQQ QALPGTPRQD GFFMPAEWAP QDAVWMLWPY RQDNWRGKAI PAQQTFAKVA
     EAISRATPVF MGVPAEFMAQ AKATMPANVT LVEMASDDAW MRDTGPTMVI NGAAERRAVD
     WQFNAWGGLN GGLYADWQQD EKVAVQVSDF LKNAHYSAPL ILEGGSIHTD GEGTLLTTAE
     CLLNPNRNPH LNQAQIEQLL CDYLGVTHFI WLQDGVYNDE TDGHIDNMCC FVRPGEVALH
     WTDDQQDPQY ARSVAAFEVL SNTVDAKGRK LKIWKLPAPG PLYNTEEETF DVLTSDAVPR
     TAGERLAGSY VNFLISNQQI IFPLLDSRTD GQANDLLQQM FPGYAIVGVP AREILLGGGN
     IHCITQQIPA A
//

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