ID   HUTG_STRPQ              Reviewed;         328 AA.
AC   P0CZ67; Q8K5L4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Formimidoylglutamase {ECO:0000255|HAMAP-Rule:MF_00737};
DE            EC=3.5.3.8 {ECO:0000255|HAMAP-Rule:MF_00737};
DE   AltName: Full=Formiminoglutamase {ECO:0000255|HAMAP-Rule:MF_00737};
DE   AltName: Full=Formiminoglutamate hydrolase {ECO:0000255|HAMAP-Rule:MF_00737};
GN   Name=hutG {ECO:0000255|HAMAP-Rule:MF_00737}; OrderedLocusNames=SPs1777;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
CC   -!- FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L-
CC       glutamate and formamide. {ECO:0000255|HAMAP-Rule:MF_00737}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-formimidoyl-L-glutamate = formamide + L-glutamate;
CC         Xref=Rhea:RHEA:22492, ChEBI:CHEBI:15377, ChEBI:CHEBI:16397,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58928; EC=3.5.3.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00737};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00737};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00737};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; L-glutamate from N-formimidoyl-L-glutamate (hydrolase
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00737}.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00737}.
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; BA000034; BAC64872.1; -; Genomic_DNA.
DR   RefSeq; WP_002982269.1; NC_004606.1.
DR   AlphaFoldDB; P0CZ67; -.
DR   SMR; P0CZ67; -.
DR   GeneID; 57853443; -.
DR   KEGG; sps:SPs1777; -.
DR   HOGENOM; CLU_039478_2_0_9; -.
DR   OMA; GTMFRQI; -.
DR   UniPathway; UPA00379; UER00552.
DR   GO; GO:0050415; F:formimidoylglutamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00737; Formimidoylglutam; 1.
DR   InterPro; IPR005923; HutG.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR11358; PTHR11358; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; SSF52768; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Histidine metabolism; Hydrolase; Manganese; Metal-binding.
FT   CHAIN           1..328
FT                   /note="Formimidoylglutamase"
FT                   /id="PRO_0000411271"
FT   BINDING         133
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         163
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         253
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         253
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         255
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
SQ   SEQUENCE   328 AA;  36373 MW;  23C6FBFA18FC748B CRC64;
     MLEDYYPSTT SYYHSGIDDD LYTAKWGMVM TFLDLNDSSL TPFEGTHFAL IGFKSDKGVY
     INNGRVGAVE SPAAIRTQLA KFPWHLGNQV MVYDVGNIDG PNRSLEQLQN SLSKAIKRMC
     DLNLKPIVLG GGHETAYGHY LGLRQSLSSS DDLAVINMDA HFDLRPYDQT GPNSGTGFRQ
     MFDDAVADKR LFKYFVLGIQ EHNNNLFLFD FVAKSKGIQF LTGQDIYQMG HQKVCRAIDR
     FLEGQERVYL TIDMDCFSVG AAPGVSAIQS LGVDPNLAVL VLQHIAASGK LVGFDVVEVS
     PPHDIDNHTA NLAATFIFYL VQIMAQHN