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HUTI_ACIBT
ID   HUTI_ACIBT              Reviewed;         401 AA.
AC   A3MA48;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 86.
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=A1S_3403;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO13792.2; -; Genomic_DNA.
DR   RefSeq; WP_000737795.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3MA48; -.
DR   SMR; A3MA48; -.
DR   KEGG; acb:A1S_3403; -.
DR   HOGENOM; CLU_041647_0_0_6; -.
DR   UniPathway; UPA00379; UER00551.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050480; F:imidazolonepropionase activity; IEA:UniProtKB-UniRule.
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: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; Zinc.
FT   CHAIN           1..401
FT                   /note="Imidazolonepropionase"
FT                   /id="PRO_0000306421"
FT   BINDING         66
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         68
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         75
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         138
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         138
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         171
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         236
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         239
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         311
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         313
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         315
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         316
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
SQ   SEQUENCE   401 AA;  44045 MW;  574D1B36BB792641 CRC64;
     MKKLWQNCHI ATMQNGQYSY IEDAAIVTEG HLIHWIGKQQ QLPADTYSET VDLNGAWVTP
     GFIDCHTHSV FGGNRSVEFE KRLQGVSYAE IAASGGGIAS TVRATREASE EQLLNSALKR
     IRCMQQDGVT TIEIKSGYGL NYENERKMLR VIRQIGEKLP MTVKSTCLAA HALPPEYKDQ
     SDAYIEHICT EMLPKLHAEG LVDAVDAFCE HLAFSPAQVE RVFKTAQSLN LPVKLHAEQL
     SSLGGSSLAA RYHALSADHL EYMTEDDVKA MAASGTVAVL LPGAFYLLRE TQYPPIESLI
     KHGVRIALSS DLNPGTSPAL SLRLMLNMGS TLFRLTPEQA LAGVTIHAAQ ALGLEQTHGS
     LEQGKVADFV AWDIEHPSEI VYWLGGDLPK RVVQHGQEVI F
 
 
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