AGUA_MYCCT
ID AGUA_MYCCT Reviewed; 364 AA.
AC Q2SRJ6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=MCAP_0652;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000123; ABC01526.1; -; Genomic_DNA.
DR RefSeq; WP_011387513.1; NC_007633.1.
DR AlphaFoldDB; Q2SRJ6; -.
DR SMR; Q2SRJ6; -.
DR EnsemblBacteria; ABC01526; ABC01526; MCAP_0652.
DR GeneID; 23778393; -.
DR KEGG; mcp:MCAP_0652; -.
DR HOGENOM; CLU_037682_1_0_14; -.
DR OMA; WCRDHGP; -.
DR OrthoDB; 771174at2; -.
DR PhylomeDB; Q2SRJ6; -.
DR Proteomes; UP000001928; 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;
KW Hydrolase.
FT CHAIN 1..364
FT /note="Putative agmatine deiminase"
FT /id="PRO_1000070558"
FT ACT_SITE 355
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ SEQUENCE 364 AA; 41566 MW; 2B14ACC70D59B033 CRC64;
MSKKMNSTPK KDGFWMPGEW EKHDQCWMIW PERSDNWRLG AKPAQRVFAN VANAIAKYEK
VTMLVSHQQF ENARNLLDQN VRVIECSNDD SWMRDVGPTI VKNKDGEIRG VDWVFNAWGG
FKGGLYFPWD KDDAIARKVC EISNIDYYRT DFVLEGGSIH TDGDGTLYTT EECLLNENRN
PDLSKEQIEE NLKEYCGVEK VIWLPLGVYN DETNGHVDNL LHVVSPGHVV LTWTDDTTDP
QYERSKLAYD ILTNTLDAKG RKIKVTKLHQ PGPLFITKEE AEGIDVCDTM SREPEQRMPA
SYANFYIANN AIILPIFGDK YDDLAVKTLQ SVYPNHKIET VMAREILLGG GNIHCITQQQ
PTTK