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HUTG_SALPB
ID   HUTG_SALPB              Reviewed;         313 AA.
AC   A9MTJ4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=SPAB_02731;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX68109.1; -; Genomic_DNA.
DR   RefSeq; WP_000195696.1; NC_010102.1.
DR   AlphaFoldDB; A9MTJ4; -.
DR   SMR; A9MTJ4; -.
DR   KEGG; spq:SPAB_02731; -.
DR   PATRIC; fig|1016998.12.peg.2584; -.
DR   HOGENOM; CLU_039478_2_0_6; -.
DR   OMA; GTMFRQI; -.
DR   BioCyc; SENT1016998:SPAB_RS11100-MON; -.
DR   UniPathway; UPA00379; UER00552.
DR   Proteomes; UP000008556; 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..313
FT                   /note="Formimidoylglutamase"
FT                   /id="PRO_1000083414"
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         241
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         241
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT   BINDING         243
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
SQ   SEQUENCE   313 AA;  34371 MW;  835206DA604469EA CRC64;
     MTQWYPASPA LWQGRDDSIE APDARRLFQT VTRSETFSPE NWQQKIALMG FACDEGVKRN
     AGRPGAAGGP DALRKALANM ASHQGHERLV DLGNWVAPTP DLEGAQQVLR DAVSRCLRAG
     MRTLVLGGGH ETAFGHGAGV LDAFAQESVG IINLDAHLDL RQTDRATSGT PFRQLAQLCD
     AQSRAFHYAC FGVSRAANTQ ALWREAQWRN VTVVEDLDCH DALAQMAQFI DKVDKIYLTI
     DLDVLPVWEM PAVSAPAALG VPLIQVLRLI EPVCRSGKLQ AADLVEFNPR FDEDGAAARV
     AARLGWQIAH WWR
 
 
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