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AGUA_SHEPC
ID   AGUA_SHEPC              Reviewed;         370 AA.
AC   A4Y946;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Putative 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=Sputcn32_2760;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the agmatine deiminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01841}.
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DR   EMBL; CP000681; ABP76479.1; -; Genomic_DNA.
DR   RefSeq; WP_011788602.1; NC_009438.1.
DR   AlphaFoldDB; A4Y946; -.
DR   SMR; A4Y946; -.
DR   STRING; 319224.Sputcn32_2760; -.
DR   GeneID; 45043249; -.
DR   KEGG; spc:Sputcn32_2760; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
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;
KW   Hydrolase.
FT   CHAIN           1..370
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_1000070570"
FT   ACT_SITE        361
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   370 AA;  40753 MW;  3C749822F11B1F72 CRC64;
     MTNVNVDVTP LTTKPSQDGF YMPAEWAAQQ AVWMIWPYRP DNWRAAGAYA QATFAKVADA
     IGAATPVYMG VPKAFLAEAK AVMPSHVTLV EMDSNDCWAR DTGPTVVVND NGECRGVDWG
     FNAWGGHNGG LYFPWDKDEQ VAQQMLAQHG FARYSAPLIL EGGSIHVDGE GTCMTSAECL
     LNANRNPELT KEQIEDLLRD YLNVKQFIWL QDGVYMDETD GHIDNMSCFA RPGEVILHWT
     DDETDPQYPR SKAALEVLQN TVDAKGRKLK IHLLPQPGPL YCSEEESKGV TEGTGVPRTA
     GERLAGSYVN FLITNHRIVF PLLDPATDDI AAQKLQEIFP EHEIVGVPAR EILLGGGNIH
     CITQQIPAGK
 
 
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