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Database: UniProt
Entry: A0A098ERE7_9BACL
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ID   A0A098ERE7_9BACL        Unreviewed;       312 AA.
AC   A0A098ERE7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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_2 {ECO:0000313|EMBL:CEG23871.1};
GN   Synonyms=hutG {ECO:0000256|HAMAP-Rule:MF_00737};
GN   ORFNames=BN1080_02878 {ECO:0000313|EMBL:CEG23871.1};
OS   Planococcus massiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG23871.1, ECO:0000313|Proteomes:UP000043699};
RN   [1] {ECO:0000313|EMBL:CEG23871.1, ECO:0000313|Proteomes:UP000043699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES2 {ECO:0000313|EMBL:CEG23871.1,
RC   ECO:0000313|Proteomes:UP000043699};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-2014) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00737}.
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DR   EMBL; CCXS01000001; CEG23871.1; -; Genomic_DNA.
DR   RefSeq; WP_052652908.1; NZ_LR698965.1.
DR   AlphaFoldDB; A0A098ERE7; -.
DR   STRING; 1499687.BN1080_02878; -.
DR   OrthoDB; 9788689at2; -.
DR   UniPathway; UPA00379; UER00552.
DR   Proteomes; UP000043699; 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   PIRSF; PIRSF036979; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00737};
KW   Reference proteome {ECO:0000313|Proteomes:UP000043699}.
SQ   SEQUENCE   312 AA;  34254 MW;  81A3150FFDDC83E2 CRC64;
     MYKLPKSHFW HGRIDSKTDR NSFYFHQAIE FLGTDEVPVE GSPFAILGFE CDEGVRRLGG
     KPGAAEASNE IRRHLADLPY HLGDRKTIDT GAVMCKGDAM EKAQRELGEH VERLLQSTIP
     IILGGGHETA YGHYLGVRRF AGPEAKIGII TIDAHFDLRD AEPPNASSMF RQILEADANS
     GVLALGIQPL ANTRTLFNKA EELGVRFVLA EEFAMGNIQQ AQSVIDAFCG EHDAVFLSLS
     MNALSSLYAP GVMAPSPFGL EPAIVRQLLW HIVANEKIIS FDLCEVNPEL DEHGKTAKLA
     AYLLAEMLAA FH
//
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