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Database: UniProt
Entry: A0A1H3NJV1_9PSEU
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ID   A0A1H3NJV1_9PSEU        Unreviewed;       316 AA.
AC   A0A1H3NJV1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN05216215_103829 {ECO:0000313|EMBL:SDY89098.1};
OS   Saccharopolyspora shandongensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=418495 {ECO:0000313|EMBL:SDY89098.1, ECO:0000313|Proteomes:UP000199529};
RN   [1] {ECO:0000313|EMBL:SDY89098.1, ECO:0000313|Proteomes:UP000199529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3530 {ECO:0000313|EMBL:SDY89098.1,
RC   ECO:0000313|Proteomes:UP000199529};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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       ECO:0000256|RuleBase:RU003684}.
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DR   EMBL; FNOK01000038; SDY89098.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3NJV1; -.
DR   STRING; 418495.SAMN05216215_103829; -.
DR   OrthoDB; 9789727at2; -.
DR   UniPathway; UPA00379; UER00552.
DR   Proteomes; UP000199529; 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   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|HAMAP-Rule:MF_00737};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00737}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         118
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
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         145
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
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         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
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   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   316 AA;  33026 MW;  3A6B49DE93D33743 CRC64;
     MSTSVPRWTG RVDGPGPEHR RWHNAIDESP GATGVSLIGF PSDIGVRRNG GRPGAQAGPG
     AIRAALGSFA IQPEVVVQDA GDVAVAGDDL EAAQDGLAEA VADQLRAGNL PVVLGGGHET
     AYGSYLGLAR SGLLDGRRLG VLNLDAHFDL READRPSSGT PFRQIAVGET ERGAEFTYAV
     IGISQPSNTA ALFATATELG VRHLHDLDCQ ERHIEDVLEF VRAFIADVDA LYLSIDLDVL
     PAAQAPGVSA PSTLGVPAAV VIEVCRLVGS DPKLALSDIT ELNSSYDIDN RTARIAARLV
     HTIVTSAADR SVPEGH
//
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