HUTG_KLEAE
ID HUTG_KLEAE Reviewed; 222 AA.
AC P19452;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Formimidoylglutamase {ECO:0000250|UniProtKB:P42068};
DE EC=3.5.3.8 {ECO:0000250|UniProtKB:P42068};
DE AltName: Full=Formiminoglutamase {ECO:0000250|UniProtKB:P42068};
DE AltName: Full=Formiminoglutamate hydrolase {ECO:0000250|UniProtKB:P42068};
DE AltName: Full=Histidine utilization protein G;
DE Flags: Fragment;
GN Name=hutG;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2203754; DOI=10.1128/jb.172.9.5477-5481.1990;
RA Schwacha A., Bender R.A.;
RT "Nucleotide sequence of the gene encoding the repressor for the histidine
RT utilization genes of Klebsiella aerogenes.";
RL J. Bacteriol. 172:5477-5481(1990).
CC -!- FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L-
CC glutamate and formamide. {ECO:0000250|UniProtKB:P42068}.
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:0000250|UniProtKB:P42068};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P42068};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P42068};
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:0000250|UniProtKB:P42068}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000305}.
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DR EMBL; M34604; AAA25074.1; -; Genomic_DNA.
DR AlphaFoldDB; P19452; -.
DR SMR; P19452; -.
DR STRING; 548.EAG7_02611; -.
DR UniPathway; UPA00379; UER00552.
DR GO; GO:0050415; F:formimidoylglutamase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
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; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Histidine metabolism; Hydrolase; Manganese; Metal-binding.
FT CHAIN <1..222
FT /note="Formimidoylglutamase"
FT /id="PRO_0000173756"
FT BINDING 34
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42068"
FT NON_TER 1
SQ SEQUENCE 222 AA; 24158 MW; 6E89A8C0FBD784A0 CRC64;
VDGEQLEAAH QALREAVADC QRAGKRTLVL GGGHETAFGH GAGVLDAFPG EKVGIINLDA
HLDLRFADCA SSGTPFRQLA LECDAQQRGF HYTCIGVSRA ANTQALWDEA ARRQVAIVED
LEVLTAFETR VLPELERNIA QFDRLYLTID LDVLPAREMP AVSAPAALGV PLGTLLRIVE
PLCRSGKLQA VDLVEFNPLF DIDGQGARAA ARVAWQIAHW WR
