HUTG_VIBCH
ID HUTG_VIBCH Reviewed; 336 AA.
AC Q9KSQ2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Formimidoylglutamase {ECO:0000255|HAMAP-Rule:MF_00737};
DE EC=3.5.3.8 {ECO:0000255|HAMAP-Rule:MF_00737};
DE AltName: Full=Formiminoglutamase {ECO:0000255|HAMAP-Rule:MF_00737};
DE AltName: Full=Formiminoglutamate hydrolase {ECO:0000255|HAMAP-Rule:MF_00737};
GN Name=hutG {ECO:0000255|HAMAP-Rule:MF_00737}; OrderedLocusNames=VC_1204;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L-
CC glutamate and formamide. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00737};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00737};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00737}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|HAMAP-
CC Rule:MF_00737}.
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DR EMBL; AE003852; AAF94363.1; -; Genomic_DNA.
DR PIR; G82228; G82228.
DR RefSeq; NP_230849.1; NC_002505.1.
DR RefSeq; WP_001069038.1; NZ_LT906614.1.
DR PDB; 1XFK; X-ray; 1.80 A; A=1-336.
DR PDBsum; 1XFK; -.
DR AlphaFoldDB; Q9KSQ2; -.
DR SMR; Q9KSQ2; -.
DR STRING; 243277.VC_1204; -.
DR DNASU; 2614637; -.
DR EnsemblBacteria; AAF94363; AAF94363; VC_1204.
DR GeneID; 57739877; -.
DR KEGG; vch:VC_1204; -.
DR PATRIC; fig|243277.26.peg.1151; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_2_0_6; -.
DR OMA; GTMFRQI; -.
DR BioCyc; VCHO:VC1204-MON; -.
DR BRENDA; 3.5.3.8; 6626.
DR UniPathway; UPA00379; UER00552.
DR EvolutionaryTrace; Q9KSQ2; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
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 GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IBA:GO_Central.
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; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01227; hutG; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Histidine metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..336
FT /note="Formimidoylglutamase"
FT /id="PRO_0000173779"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 157
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 157
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 159
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:1XFK"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1XFK"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1XFK"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1XFK"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:1XFK"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1XFK"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1XFK"
FT HELIX 310..332
FT /evidence="ECO:0007829|PDB:1XFK"
SQ SEQUENCE 336 AA; 37329 MW; EBC94AF053A98696 CRC64;
MNPNFTTEHT WQGRHDPEDG QAGRRVHHIA CPIQVGELAN QEPGVALIGF ECDAGVERNK
GRTGAKHAPS LIKQALANLA WHHPIPIYDL GNIRCEGDEL EQAQQECAQV IQQALPHARA
IVLGGGHEIA WATFQGLAQH FLATGVKQPR IGIINFDAHF DLRTFESELA PVRPSSGTPF
NQIHHFCQQQ GWDFHYACLG VSRASNTPAL FERADKLGVW YVEDKAFSPL SLKDHLTQLQ
HFIDDCDYLY LTIDLDVFPA ASAPGVSAPA ARGVSLEALA PYFDRILHYK NKLMIADIAE
YNPSFDIDQH TARLAARLCW DIANAMAEQV QSIRHP
