HUTG_PSEAE
ID HUTG_PSEAE Reviewed; 311 AA.
AC Q9HZ59;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=PA3175;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; AE004091; AAG06563.1; -; Genomic_DNA.
DR PIR; G83249; G83249.
DR RefSeq; NP_251865.1; NC_002516.2.
DR RefSeq; WP_003113438.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; Q9HZ59; -.
DR SMR; Q9HZ59; -.
DR STRING; 287.DR97_4761; -.
DR PaxDb; Q9HZ59; -.
DR PRIDE; Q9HZ59; -.
DR EnsemblBacteria; AAG06563; AAG06563; PA3175.
DR GeneID; 882685; -.
DR KEGG; pae:PA3175; -.
DR PATRIC; fig|208964.12.peg.3318; -.
DR PseudoCAP; PA3175; -.
DR HOGENOM; CLU_039478_2_0_6; -.
DR InParanoid; Q9HZ59; -.
DR OMA; GTMFRQI; -.
DR PhylomeDB; Q9HZ59; -.
DR BioCyc; PAER208964:G1FZ6-3235-MON; -.
DR UniPathway; UPA00379; UER00552.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR GO; GO:0050415; F:formimidoylglutamase activity; IDA:PseudoCAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006548; P:histidine catabolic process; IMP:PseudoCAP.
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 PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01227; hutG; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Histidine metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..311
FT /note="Formimidoylglutamase"
FT /id="PRO_0000173762"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737"
SQ SEQUENCE 311 AA; 34231 MW; B69B29F52502F11E CRC64;
MYPAPDMSLW QGRIDSQEGA DARRWHQWMR PYADDAEAAS VLLGFASDEG VRRNQGRQGA
RHGPPALRRA LANLAWHGEQ AIYDAGDIVA GDDLEAAQEC YAQRVADLLA CGHRVVGLGG
GHEIAYASFA GLARHLSRHE RLPRIGILNF DAHFDLRHAE RASSGTPFRQ IAELCQASDW
PFAYCCLGIS RLSNTAALFD QAQRLGVRYL LDRQLQPWNL ERSEAFLDGF LQSVDHLYLT
VCLDVLPAAQ APGVSAPSAH GVEMPVVEHL VRRAKASGKL RLADIAELNP QLDSDQRTAR
IAARLVDSLV N
