ID A0A1S1HK28_PROST Unreviewed; 305 AA.
AC A0A1S1HK28;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Formimidoylglutamase {ECO:0000256|HAMAP-Rule:MF_00737, ECO:0000256|NCBIfam:TIGR01227};
DE EC=3.5.3.8 {ECO:0000256|HAMAP-Rule:MF_00737, ECO:0000256|NCBIfam:TIGR01227};
DE AltName: Full=Formiminoglutamase {ECO:0000256|HAMAP-Rule:MF_00737};
DE AltName: Full=Formiminoglutamate hydrolase {ECO:0000256|HAMAP-Rule:MF_00737};
GN Name=hutG {ECO:0000256|HAMAP-Rule:MF_00737,
GN ECO:0000313|EMBL:EMJ5135687.1};
GN ORFNames=A3Q29_11410 {ECO:0000313|EMBL:OHT22408.1}, RG298_003449
GN {ECO:0000313|EMBL:EMJ5135687.1};
OS Providencia stuartii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Morganellaceae; Providencia.
OX NCBI_TaxID=588 {ECO:0000313|EMBL:OHT22408.1, ECO:0000313|Proteomes:UP000179588};
RN [1] {ECO:0000313|EMBL:OHT22408.1, ECO:0000313|Proteomes:UP000179588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Crippen {ECO:0000313|EMBL:OHT22408.1,
RC ECO:0000313|Proteomes:UP000179588};
RA Yuan Y., Zhang Y., Fu S., Crippen T.L., Visi D., Benbow M.E., Allen M.,
RA Tomberlin J.K., Sze S.-H., Tarone A.M.;
RT "Genome sequence of Providencia stuartii strain, isolated from the salivary
RT glands of larval Lucilia sericata.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EMJ5135687.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2021GO-0154 {ECO:0000313|EMBL:EMJ5135687.1};
RG Clinical and Environmental Microbiology Branch: Whole genome sequencing antimicrobial resistance pathogens in the healthcare setting;
RL Submitted (FEB-2024) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L-
CC glutamate and formamide. {ECO:0000256|HAMAP-Rule:MF_00737}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-formimidoyl-L-glutamate + H2O = 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:0000256|HAMAP-Rule:MF_00737};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00737,
CC ECO:0000256|PIRSR:PIRSR036979-1};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00737, ECO:0000256|PIRSR:PIRSR036979-1};
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:0000256|HAMAP-Rule:MF_00737}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|HAMAP-
CC Rule:MF_00737, ECO:0000256|PROSITE-ProRule:PRU00742,
CC ECO:0000256|RuleBase:RU003684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHT22408.1}.
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DR EMBL; ABMABF030000013; EMJ5135687.1; -; Genomic_DNA.
DR EMBL; LVIE01000234; OHT22408.1; -; Genomic_DNA.
DR RefSeq; WP_070930028.1; NZ_CANMXG010000003.1.
DR AlphaFoldDB; A0A1S1HK28; -.
DR GeneID; 92278469; -.
DR OrthoDB; 9789727at2; -.
DR UniPathway; UPA00379; UER00552.
DR Proteomes; UP000179588; Unassembled WGS sequence.
DR GO; GO:0008783; F:agmatinase activity; IEA:TreeGrafter.
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:L-histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniRule.
DR GO; GO:0019557; P:L-histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, via agmatine; IEA:TreeGrafter.
DR CDD; cd09988; Formimidoylglutamase; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR HAMAP; MF_00737; Formimidoylglutam; 1.
DR InterPro; IPR005923; HutG.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR01227; hutG; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR PANTHER; PTHR11358:SF35; FORMIMIDOYLGLUTAMASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW Rule:MF_00737};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00737};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00737};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00737}; Reference proteome {ECO:0000313|Proteomes:UP000179588}.
FT BINDING 116
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737,
FT ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737,
FT ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737,
FT ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737,
FT ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
SQ SEQUENCE 305 AA; 33591 MW; 10ECFD74C11F8DAE CRC64;
MAAPFIWQGR TDGDTEEHLR IHQVMNKNTP AQFALIGFAS DEGVRRNKGR LGAKAGPDAI
RQQLAGLPLH QPLAIRDAGT VRCDDNDLET AQRNLSDQLI AILSSNQTPI VLGGGHEVAF
ASFQGLFDFV AQTEPTKTIG IINFDAHFDL RTAMEATSGT PFLQSAKLCE QHNRPFNYLC
LGIADHGNTK VLFDTADKLG CQYIRDRELS QSQLPKAINQ IQQFIEQVDY LYVTVDLDVF
SASIAPGVSA PAAKGINTET FDELFAVIKA SQKIAVFDIA ECNPEFDIDN HTSKLAAYLI
YQFLF
//
