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Entry: U3GXL5_9CORY
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Original site: U3GXL5_9CORY 
ID   U3GXL5_9CORY            Unreviewed;       393 AA.
AC   U3GXL5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Imidazolonepropionase {ECO:0000256|ARBA:ARBA00012864, ECO:0000256|HAMAP-Rule:MF_00372};
DE            EC=3.5.2.7 {ECO:0000256|ARBA:ARBA00012864, ECO:0000256|HAMAP-Rule:MF_00372};
DE   AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000256|HAMAP-Rule:MF_00372};
GN   Name=hutI {ECO:0000256|HAMAP-Rule:MF_00372};
GN   ORFNames=CARG_03145 {ECO:0000313|EMBL:AGU14781.1};
OS   Corynebacterium argentoratense DSM 44202.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU14781.1, ECO:0000313|Proteomes:UP000016943};
RN   [1] {ECO:0000313|EMBL:AGU14781.1, ECO:0000313|Proteomes:UP000016943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU14781.1};
RX   PubMed=24092787;
RA   Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA   Ruckert C., Tauch A.;
RT   "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT   argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL   Genome Announc. 1:e00793-13(2013).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00372};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00372};
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00372};
CC       Note=Binds 1 zinc or iron ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00372}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       HutI family. {ECO:0000256|HAMAP-Rule:MF_00372}.
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DR   EMBL; CP006365; AGU14781.1; -; Genomic_DNA.
DR   RefSeq; WP_020975932.1; NC_022198.1.
DR   AlphaFoldDB; U3GXL5; -.
DR   STRING; 1348662.CARG_03145; -.
DR   GeneID; 78249452; -.
DR   KEGG; caz:CARG_03145; -.
DR   PATRIC; fig|1348662.3.peg.619; -.
DR   eggNOG; COG1228; Bacteria.
DR   HOGENOM; CLU_041647_1_0_11; -.
DR   OrthoDB; 9776455at2; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000016943; Chromosome.
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   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   HAMAP; MF_00372; HutI; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR005920; HutI.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01224; hutI; 1.
DR   PANTHER; PTHR42752; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR42752:SF1; IMIDAZOLONEPROPIONASE-RELATED; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372};
KW   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW   Rule:MF_00372};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00372};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00372};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00372}; Reference proteome {ECO:0000313|Proteomes:UP000016943};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00372}.
FT   DOMAIN          95..366
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          328..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         66
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         73
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         131
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         131
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         158
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         219
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         222
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         293
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         295
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         297
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         298
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
SQ   SEQUENCE   393 AA;  41309 MW;  2B6FF5EBDB3133F6 CRC64;
     MSSTLFTGIS ELHTVSERGV INNGAVIIQD GTIQWVGPAA EAPAADQEID CGGRAVLPGW
     VDSHTHMIFA GDRSQEFAAR MAGEDYAAGG IAVTMNATRE AGEHALTELL KQRIRDAHAG
     GTTTIETKTG YGLDTQSEAL AARIAAAHVD DVTFLGAHLV PPGADPDTYL DEVCGPMLDA
     VAPHAQWIDV FCERGAFNEE QSRRVLRAGQ ARGLKPRVHG NQLGEGSGVQ LAVELGAASV
     DHVNYINAED IEALASSNTV ATVLPACDLS TRQPLAPART LIDAGVHLAI ASNLNPGTSY
     TSSMNFCVGT AVLQMHLSLE EAIRAGTSGG ARALERHDTG NGLDPHRRPA KGTLVEGAAA
     DLHILCSAHA IDLAYRPGMP MTHQTYRAGR RVA
//
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