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AGUA_MARMS
ID   AGUA_MARMS              Reviewed;         369 AA.
AC   A6VVD9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=Mmwyl1_1489;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
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., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-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; CP000749; ABR70418.1; -; Genomic_DNA.
DR   RefSeq; WP_012069203.1; NC_009654.1.
DR   AlphaFoldDB; A6VVD9; -.
DR   SMR; A6VVD9; -.
DR   STRING; 400668.Mmwyl1_1489; -.
DR   EnsemblBacteria; ABR70418; ABR70418; Mmwyl1_1489.
DR   KEGG; mmw:Mmwyl1_1489; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   OrthoDB; 771174at2; -.
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..369
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_1000088465"
FT   ACT_SITE        355
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   369 AA;  41366 MW;  C38CDD00575FCE3A CRC64;
     MSSTLYTSPR LDGFRMPAEH EPQEQVWMAW PTREDNWREK GKHAQAEFVA VATAIAQSTK
     VTFIVDAKHY EQARLALPDQ IRVIEIPSDD CWMRDIGATY VVNDQGERRA NSWQFNAWGG
     ELDGLYDSWE QDNAVAEKMA AVTGDYVYHA PLILEGGSIH VDGEGTLYTT EECLLHPSRN
     PHLSKEDIED LLKVYLNVEK IIWLKDGLYN DETNGHVDNI MHVIRPGVVA LTDCEDSNDP
     QYAISKAAIK VLSQAIDAKG RTLEIIKLPM PGPLFVSEDE AKNLLKSDSM NRQVGERLAA
     SYANFLITNN SIVFPTFGEK TDEQAKEILQ KAFPEHKVIG VYARNILLGG GNIHCITQQV
     PEKCSIKVV
 
 
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