ID A0A1W9SX93_9BACT Unreviewed; 336 AA.
AC A0A1W9SX93;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=Formimidoylglutamase {ECO:0000256|HAMAP-Rule:MF_00737};
DE EC=3.5.3.8 {ECO:0000256|HAMAP-Rule:MF_00737};
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 ORFNames=B6I20_07805 {ECO:0000313|EMBL:OQY01303.1};
OS Bacteroidetes bacterium 4572_117.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1971632 {ECO:0000313|EMBL:OQY01303.1, ECO:0000313|Proteomes:UP000192701};
RN [1] {ECO:0000313|Proteomes:UP000192701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) 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=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:0000256|HAMAP-Rule:MF_00737};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00737};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|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: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 -!- 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:OQY01303.1}.
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DR EMBL; NBLH01000109; OQY01303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9SX93; -.
DR UniPathway; UPA00379; UER00552.
DR Proteomes; UP000192701; Unassembled WGS sequence.
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 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 NCBIfam; TIGR01227; hutG; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR PANTHER; PTHR11358:SF35; FORMIMIDOYLGLUTAMASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 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}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00737};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00737};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00737}.
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
SQ SEQUENCE 336 AA; 37658 MW; FCD296C52B591216 CRC64;
MVNNYRVANK NIWQGRVDNS KDFASFRWHQ VICNINLSNL GETKIDINKK NYCLLGYECN
EGVIRNLGRT GTEKAPDYLR KEMANLAWNN NSNVELYDAG NIFCLNNNLE TAQQALSEAV
EKILSLGMFP IIMGGGHDIA FGNYNGVAGF VYKRQKEKRI GIINFDAHFD LRPYKNMKGS
SGTMFLQIAD MCKKNNNAFS YHCVGIQTYA NTKRLFQTAK ELNVNFELAK NINESNLADI
KSNLNKFISQ NDHIYLTICS DVFSSAYAPG VSSPQPFGLL PEISLELIKY VAASNKLVSF
DIAEISPRFD EDNRTAKLGA IIIYALINTL SGNHLG
//