ID A0A437QB20_9GAMM Unreviewed; 339 AA.
AC A0A437QB20;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:RVU31736.1};
GN ORFNames=EOE65_07085 {ECO:0000313|EMBL:RVU31736.1};
OS Neptunomonas marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Neptunomonas.
OX NCBI_TaxID=1815562 {ECO:0000313|EMBL:RVU31736.1, ECO:0000313|Proteomes:UP000282818};
RN [1] {ECO:0000313|EMBL:RVU31736.1, ECO:0000313|Proteomes:UP000282818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPM-16 {ECO:0000313|EMBL:RVU31736.1,
RC ECO:0000313|Proteomes:UP000282818};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVU31736.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SACQ01000002; RVU31736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437QB20; -.
DR UniPathway; UPA00379; UER00552.
DR Proteomes; UP000282818; 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};
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|HAMAP-Rule:MF_00737};
KW Reference proteome {ECO:0000313|Proteomes:UP000282818}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 157
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 159
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00737"
SQ SEQUENCE 339 AA; 36534 MW; 98AE5154248A5CD3 CRC64;
MKRVLPPAPW QGRNDQDQPE HAKRWHHQVE IQTDAHMPID VTHGLIGFCC DAGVRRNHGR
PGAAEGPAAF RRQLANLACH DTAVRLGDFG DVIAEGDELE AAQATLANSV AQVLSHTDIS
RLLVVGGGHE TAWGSFCGLY QALGPDVRIG IINLDAHFDL RKPEAQGPSS GTPFYQIREL
VGADNFFYTC LGVAQESNTA TLFQRATEWG VHYRADHEMT AAHLPAICDE IDAFTQSVDA
LYLTIDLDVL PHYQAPGVSA PASRGVSLAV IEAVIAQIKQ SAQHCRLGLP LVELTELNPS
CDLQGVTART AAILANALLS DSASAGKPVR DLTPLIERK
//
