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AGUA_ENTFA
ID   AGUA_ENTFA              Reviewed;         365 AA.
AC   Q837U5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative agmatine deiminase {ECO:0000255|HAMAP-Rule:MF_01841};
DE            EC=3.5.3.12 {ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272};
DE   AltName: Full=Agmatine iminohydrolase {ECO:0000255|HAMAP-Rule:MF_01841};
GN   Name=aguA {ECO:0000255|HAMAP-Rule:MF_01841}; OrderedLocusNames=EF_0734;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), CATALYTIC ACTIVITY, ACTIVE SITE,
RP   AND SUBUNIT.
RX   PubMed=17028272; DOI=10.1128/jb.01216-06;
RA   Llacer J.L., Polo L.M., Tavarez S., Alarcon B., Hilario R., Rubio V.;
RT   "The gene cluster for agmatine catabolism of Enterococcus faecalis: study
RT   of recombinant putrescine transcarbamylase and agmatine deiminase and a
RT   snapshot of agmatine deiminase catalyzing its reaction.";
RL   J. Bacteriol. 189:1254-1265(2007).
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         ECO:0000269|PubMed:17028272};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18038;
CC         Evidence={ECO:0000269|PubMed:17028272};
CC   -!- SUBUNIT: Tetramer of two homodimers. {ECO:0000269|PubMed:17028272}.
CC   -!- SIMILARITY: Belongs to the agmatine deiminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01841}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO80553.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAO80553.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE016830; AAO80553.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_814483.2; NC_004668.1.
DR   RefSeq; WP_002363185.1; NZ_KE136527.1.
DR   PDB; 2JER; X-ray; 1.65 A; A/B/C/D/E/F/G/H=1-365.
DR   PDBsum; 2JER; -.
DR   AlphaFoldDB; Q837U5; -.
DR   SMR; Q837U5; -.
DR   STRING; 226185.EF_0734; -.
DR   EnsemblBacteria; AAO80553; AAO80553; EF_0734.
DR   KEGG; efa:EF0734; -.
DR   PATRIC; fig|226185.45.peg.2675; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_0_0_9; -.
DR   OMA; GNVACIT; -.
DR   BRENDA; 3.5.3.12; 2095.
DR   SABIO-RK; Q837U5; -.
DR   EvolutionaryTrace; Q837U5; -.
DR   Proteomes; UP000001415; 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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..365
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194324"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841,
FT                   ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER"
FT   BINDING         214
FT                   /ligand="agmatine"
FT                   /ligand_id="ChEBI:CHEBI:58145"
FT                   /evidence="ECO:0000250|UniProtKB:G7JT50"
FT   BINDING         220
FT                   /ligand="agmatine"
FT                   /ligand_id="ChEBI:CHEBI:58145"
FT                   /evidence="ECO:0000250|UniProtKB:G7JT50"
FT   HELIX           10..13
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          24..30
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           43..57
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           71..77
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          109..115
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           136..144
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          165..172
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   TURN            179..181
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           187..198
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          201..206
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   TURN            212..215
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           244..255
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          266..270
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          308..310
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           324..334
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          338..344
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           346..349
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   TURN            350..352
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   HELIX           356..358
FT                   /evidence="ECO:0007829|PDB:2JER"
FT   STRAND          360..363
FT                   /evidence="ECO:0007829|PDB:2JER"
SQ   SEQUENCE   365 AA;  41199 MW;  9B8ABD927D92AD58 CRC64;
     MAKRIVGSTP KQDGFRMPGE FEPQEKVWMI WPERPDNWRD GGKPVQEAFT NVAKAISQFT
     PMNVVVSQQQ FQNCRRQLPP EITVYEMSNN DAWVRDCGPS FVINDHGEIR GVDWTFNAWG
     GLVDGLYFPW DQDDLVAQKI CEIEHVDSYR TDDFVLEGGS FHVDGQGTVL TTEMCLLSEG
     RNPQLSKEAI EQKLCDYLNV EKVLWLGDGI DPEETNGHVD DVACFIAPGE VACIYTEDQN
     SPFYEAAQDA YQRLLKMTDA KGRQLKVHKL CCPVKNVTIK GSFKIDFVEG TMPREDGDIC
     IASYMNFLIT NDGVIVPQYG DENDHLALEQ VQTMFPDKKI VGVNTVEVVY GGGNIHCITQ
     QEPKR
 
 
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