ID   AGUA_STRZT              Reviewed;         361 AA.
AC   C1CRX2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=SPT_1278;
OS   Streptococcus pneumoniae (strain Taiwan19F-14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Taiwan19F-14;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000921; ACO24000.1; -; Genomic_DNA.
DR   RefSeq; WP_000969458.1; NC_012469.1.
DR   AlphaFoldDB; C1CRX2; -.
DR   SMR; C1CRX2; -.
DR   KEGG; snt:SPT_1278; -.
DR   HOGENOM; CLU_037682_1_0_9; -.
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..361
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_1000188421"
FT   ACT_SITE        354
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   361 AA;  40408 MW;  ED755F7D9C96B819 CRC64;
     MMDSPKKLGY HMPAEYEPHH GTLMIWPTRP GSWPFQGKAA KRAFTQIIET IAEGERVYLL
     VEQAYLYEAQ SYLGDKVVYL DIPTNDAWAR DTGPTILVND KGKKLAVDWA FNAWGGTYDG
     LYQDYEEDDQ VASRFAEVLE KPVYDAKPFV LEGGAIHSDG QGTILVTESC LLSPGRNPNL
     TKEEIENTLL ESLGAEKVIW LPYGIYQDET NEHVDNVAAF VGSAELVLAW TDDENDPQYA
     MSKADLELLE QETDAKGCHF TIHKLPIPAV RQVVTEEDLP GYIYEEGEEE RYAGERLAAS
     YVNFYIANKA VLVPQFEDVN DQVAIDILSK CFPDRKVVGI PARDILLGGG NIHCITQQIP
     E