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HUTI_SALTY
ID   HUTI_SALTY              Reviewed;         407 AA.
AC   Q8ZQR2;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Imidazolonepropionase {ECO:0000255|HAMAP-Rule:MF_00372};
DE            EC=3.5.2.7 {ECO:0000255|HAMAP-Rule:MF_00372};
DE   AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00372};
GN   Name=hutI {ECO:0000255|HAMAP-Rule:MF_00372}; OrderedLocusNames=STM0787;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond
CC       in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is
CC       the third step in the universal histidine degradation pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_00372}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate;
CC         Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377, ChEBI:CHEBI:58928,
CC         ChEBI:CHEBI:77893; EC=3.5.2.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00372};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00372};
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00372};
CC       Note=Binds 1 zinc or iron ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00372};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00372}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00372}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       HutI family. {ECO:0000255|HAMAP-Rule:MF_00372}.
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DR   EMBL; AE006468; AAL19725.1; -; Genomic_DNA.
DR   RefSeq; NP_459766.1; NC_003197.2.
DR   RefSeq; WP_001249472.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZQR2; -.
DR   SMR; Q8ZQR2; -.
DR   STRING; 99287.STM0787; -.
DR   PaxDb; Q8ZQR2; -.
DR   EnsemblBacteria; AAL19725; AAL19725; STM0787.
DR   GeneID; 1252307; -.
DR   KEGG; stm:STM0787; -.
DR   PATRIC; fig|99287.12.peg.820; -.
DR   HOGENOM; CLU_041647_0_0_6; -.
DR   OMA; MVYEPGR; -.
DR   PhylomeDB; Q8ZQR2; -.
DR   BioCyc; SENT99287:STM0787-MON; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050480; F:imidazolonepropionase activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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; cd01296; Imidazolone-5PH; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_00372; HutI; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR005920; HutI.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR42752; PTHR42752; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01224; hutI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Histidine metabolism; Hydrolase; Iron; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..407
FT                   /note="Imidazolonepropionase"
FT                   /id="PRO_0000160957"
FT   BINDING         74
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         76
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         83
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         146
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         146
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         179
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         244
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         247
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         319
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         321
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         323
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         324
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
SQ   SEQUENCE   407 AA;  44629 MW;  FFD00FE8C5AA0D01 CRC64;
     MRQLLPGDTV WRNIRLATMD PQQQALYGLV DNQALIVREG HICDIVPETQ LPVSGDNIHD
     MQGRLVTPGL IDCHTHLVFA GNRAAEWEQR LNGASYQHIS AQGGGINATV SATRACAEET
     LYLLARERMM RLASEGVTLL EIKSGYGLEL ATEEKLLRVA AKLAAENAID ISPTLLAAHA
     TPAEYRDDPD GYITLVCETM IPQLWQKGLF DAVDLFCESV GFNVAQSERV LQTAKALGIP
     VKGHVEQLSL LGGAQLVSRY QGLSADHIEY LDEVGVAAMR DGGTVGVLLP GAFYFLRETQ
     RPPVELLRRY QVPVAVASDF NPGTSPFCSL HLAMNMACVQ FGLTPEEAWA GVTRHAARAL
     GRQATHGQIR AGYRADFVVW DAEQPVEIVY EPGRNPLYQR VYRGKIS
 
 
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