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Database: UniProt
Entry: A0A1W9SX93_9BACT
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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
//
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