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AGUA_PHOPR
ID   AGUA_PHOPR              Reviewed;         363 AA.
AC   Q6LG16;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 79.
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}; OrderedLocusNames=PBPRB1916;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG23764.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CR378681; CAG23764.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q6LG16; -.
DR   SMR; Q6LG16; -.
DR   STRING; 298386.PBPRB1916; -.
DR   EnsemblBacteria; CAG23764; CAG23764; PBPRB1916.
DR   KEGG; ppr:PBPRB1916; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_2_1_6; -.
DR   Proteomes; UP000000593; Chromosome 2.
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; Reference proteome.
FT   CHAIN           1..363
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194336"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        355
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   363 AA;  40680 MW;  0AF530773E5F5AA7 CRC64;
     MTKQLSTSPK QDGFRMPAEH EPQSAIWMAW PERTDNWRYG AKPAQATFVE VAKAIAKTTP
     VTMVVSAEQF ENARVVLPSY IQVLEMSTDD SWMRDIGPSY VVNDHGKRRG VDWHFNALGQ
     IGDGLYSPWD KDDAVARKVC ETLGDDSYRA PIVLEGGSIH VDGEGTLYTT EECLLHPSRN
     PDLTREEIED VLKVTLSIEK VIWIPQGLYN DETNGHVDNL IHVVRPGEIA LTWCDDETDP
     QYLISRKAMD VLLTETDAKG RQIKIHKLPM PGPLYISEDE ANGVDVSEGM ERVPGERLAG
     SYANYLISNE HIIYPLLDEK HDKDVAMLLA KLYPNYEVTG VNAREILLGG GNIHCITQQI
     PKV
 
 
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