HUTG_STAHJ
ID HUTG_STAHJ Reviewed; 311 AA.
AC Q4L8J3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SH0723;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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}.
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DR EMBL; AP006716; BAE04032.1; -; Genomic_DNA.
DR RefSeq; WP_011275047.1; NC_007168.1.
DR AlphaFoldDB; Q4L8J3; -.
DR SMR; Q4L8J3; -.
DR STRING; 279808.SH0723; -.
DR EnsemblBacteria; BAE04032; BAE04032; SH0723.
DR GeneID; 58063089; -.
DR KEGG; sha:SH0723; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_2_0_9; -.
DR OMA; GTMFRQI; -.
DR OrthoDB; 1598732at2; -.
DR UniPathway; UPA00379; UER00552.
DR Proteomes; UP000000543; Chromosome.
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 SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01227; hutG; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Histidine metabolism; Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..311
FT /note="Formimidoylglutamase"
FT /id="PRO_0000173774"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 157
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
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 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
SQ SEQUENCE 311 AA; 34905 MW; E1463AAEAABC1483 CRC64;
MYTQGNPKLW TGRLDSETDP KQFRHFQTVK FANLENMENV SDKTGVGLLG YAVDKGVENN
KGRIGSRKGP DIIKHEFAKL PDLSECEMLI DYGNVEHTSN HLRETQQEMA RLSAKVIKQH
KQAFLIGGGH DIAYAQYLAT REVYSDASIG IINIDAHFDT RPDEPPTSGT MFREILDNDE
NVDYLVLGLA QGGNTRALYD YAKDNNIIYV YADELLHQVS PTIKDKIERF IHDHDTIMFT
ICMDVIDSAF APGVSSPSVL GLYPHSVFEI SKRVILSDKV SSISIAETNP DYDVDNRTSK
LAANLIHHFL V
