HUTU_PSESX
ID HUTU_PSESX Reviewed; 565 AA.
AC Q9AGU4;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Urocanate hydratase {ECO:0000255|HAMAP-Rule:MF_00577};
DE Short=Urocanase {ECO:0000255|HAMAP-Rule:MF_00577};
DE EC=4.2.1.49 {ECO:0000255|HAMAP-Rule:MF_00577};
DE AltName: Full=Imidazolonepropionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00577};
GN Name=hutU {ECO:0000255|HAMAP-Rule:MF_00577};
OS Pseudomonas syringae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Lz4W;
RX PubMed=11772602; DOI=10.1128/aem.68.1.1-10.2002;
RA Janiyani K.L., Ray M.K.;
RT "Cloning, sequencing, and expression of the cold-inducible hutU gene from
RT the antarctic psychrotrophic bacterium Pseudomonas syringae.";
RL Appl. Environ. Microbiol. 68:1-10(2002).
CC -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5-
CC propionate. {ECO:0000255|HAMAP-Rule:MF_00577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-imidazolone-5-propanoate = H2O + trans-urocanate;
CC Xref=Rhea:RHEA:13101, ChEBI:CHEBI:15377, ChEBI:CHEBI:17771,
CC ChEBI:CHEBI:77893; EC=4.2.1.49; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00577};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00577};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00577};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
CC {ECO:0000255|HAMAP-Rule:MF_00577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00577}.
CC -!- INDUCTION: By cold.
CC -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000255|HAMAP-
CC Rule:MF_00577, ECO:0000305}.
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DR EMBL; AF326719; AAK15634.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AGU4; -.
DR SMR; Q9AGU4; -.
DR PRIDE; Q9AGU4; -.
DR eggNOG; COG2987; Bacteria.
DR UniPathway; UPA00379; UER00550.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016153; F:urocanate hydratase activity; 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; 3.40.50.10730; -; 1.
DR HAMAP; MF_00577; HutU; 1.
DR InterPro; IPR023637; Urocanase.
DR InterPro; IPR035401; Urocanase_C.
DR InterPro; IPR038364; Urocanase_central_sf.
DR InterPro; IPR023636; Urocanase_CS.
DR InterPro; IPR035400; Urocanase_N.
DR InterPro; IPR035085; Urocanase_Rossmann-like.
DR InterPro; IPR036190; Urocanase_sf.
DR PANTHER; PTHR12216; PTHR12216; 1.
DR Pfam; PF01175; Urocanase; 1.
DR Pfam; PF17392; Urocanase_C; 1.
DR Pfam; PF17391; Urocanase_N; 1.
DR PIRSF; PIRSF001423; Urocanate_hydrat; 1.
DR SUPFAM; SSF111326; SSF111326; 1.
DR TIGRFAMs; TIGR01228; hutU; 1.
DR PROSITE; PS01233; UROCANASE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Histidine metabolism; Lyase; NAD; Stress response.
FT CHAIN 1..565
FT /note="Urocanate hydratase"
FT /id="PRO_0000207347"
FT REGION 453..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 419
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 61..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 185..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 251..252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 272..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 282..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 331
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 501
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
SQ SEQUENCE 565 AA; 61334 MW; 8065B024DF5172B6 CRC64;
MTSTTPKSPA AFTRHRDGEI RAARGTQLTA KSWMTEAPLR MLMNNLDPQV AENPTELVVY
GGIGRAARNW ECYDKIVESL TNLNDDETLL VQSGKPVGVF KTHSNAPRVL IANSNLVPHW
ATWEHFNELD AKGLAMYGQM TAGSWINIGS QGIVQGTYET FVEAGRQHYN GSLKGKWVLT
AGLGGMGGAQ PLAATLAGAC SLNIECQQSR IDFRLATRYV DEQALDLDDA LVRIAKYTAE
GKAISIALCG NAAELLPEMV RRGVRPDMVT DQTSAHDPLN GYLPKGWTWE QYRDRAVTDP
AAVVKAAKAS MGEHVEAMLA FQKAGIPTFD YGNNIRQMAK EVGVENAFDF PGFVPAYIRP
LFCRGVGPFR WVALSGDAED IYKTDAKVKE LIADDAHLHN WLDMARERIS FQGLPARICW
VGLGQRAKLG LAFNEMVRSG ELKAPIVIGR DHLDSGSVSS PNRETESMKD GSDAVSDWPL
LNALLNTASG ATWVSLHHGG GVGMGFSQHS GMVIVCDGTD EAAERIARVL HNDPATGVMR
HADAGYDIAI DCANEQGLNL PMING
