ID F8E3E1_CORRG Unreviewed; 351 AA.
AC F8E3E1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 ECO:0000313|EMBL:AEI10467.1};
GN OrderedLocusNames=CRES_2114 {ECO:0000313|EMBL:AEI10467.1};
OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS 158).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI10467.1, ECO:0000313|Proteomes:UP000000492};
RN [1] {ECO:0000313|EMBL:AEI10467.1, ECO:0000313|Proteomes:UP000000492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC {ECO:0000313|Proteomes:UP000000492};
RX PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA Schneider J., Trost E., Tauch A.;
RT "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT samples of a leukemia patient.";
RL BMC Genomics 13:141-141(2012).
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; CP002857; AEI10467.1; -; Genomic_DNA.
DR RefSeq; WP_013889446.1; NC_015673.1.
DR AlphaFoldDB; F8E3E1; -.
DR STRING; 662755.CRES_2114; -.
DR KEGG; crd:CRES_2114; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_2_0_11; -.
DR OrthoDB; 9789727at2; -.
DR UniPathway; UPA00379; UER00552.
DR Proteomes; UP000000492; Chromosome.
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 PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR PANTHER; PTHR11358:SF35; FORMIMIDOYLGLUTAMASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 2.
DR PRINTS; PR00116; ARGINASE.
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}; Reference proteome {ECO:0000313|Proteomes:UP000000492}.
FT REGION 148..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 188
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
SQ SEQUENCE 351 AA; 36929 MW; 6C5856BBEC90A3E3 CRC64;
MNTVDELPLF SEPGEWKGRV DGPGPEHARW NSVITSAADD THDAVALLGY ASDEGVLRNS
GRQGAAAGPE AIRGVLGSLA IHDDHPRVDA GTVCTQGDDL EGSQEELSQR VQQLIAKNNL
VVVLGGGHET SFATHRGLHR ALHSKGLETG SAHDEQSSIE QSTFEQGSES AGATDEVGST
GIVNLDAHFD LRSAEKPTSG TPFLQIAELV GDKFDYHVWG ISKPNNTKVL FDTADRLGAR
VVLDEELLAM TPQQVANLAT ATCHEHEHIH LSIDLDVLPA NEAPGVSAPA GLGVPLSHIR
AAAKAIAATG KVRLVDVVEL NPSVDVDNRT ARVAARLIDD IVAAAIAAKA N
//
