HUTU_GEOKA
ID HUTU_GEOKA Reviewed; 551 AA.
AC Q5L084;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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}; OrderedLocusNames=GK1367;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2] {ECO:0007744|PDB:1X87}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH NAD, AND COFACTOR.
RA Tereshko V., Zaborske J., Gilbreth R., Dementieva I., Collart F.,
RA Joachimiak A., Kossiakoff A.;
RT "2.4A x-ray structure of urocanase protein complexed with NAD.";
RL Submitted (AUG-2004) to the PDB data bank.
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, ECO:0000269|Ref.2};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00577,
CC ECO:0000269|Ref.2};
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 -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000255|HAMAP-
CC Rule:MF_00577}.
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DR EMBL; BA000043; BAD75652.1; -; Genomic_DNA.
DR PDB; 1X87; X-ray; 2.40 A; A/B=1-551.
DR PDBsum; 1X87; -.
DR AlphaFoldDB; Q5L084; -.
DR SMR; Q5L084; -.
DR STRING; 235909.GK1367; -.
DR EnsemblBacteria; BAD75652; BAD75652; GK1367.
DR KEGG; gka:GK1367; -.
DR eggNOG; COG2987; Bacteria.
DR HOGENOM; CLU_018868_0_1_9; -.
DR OMA; LVGDWAN; -.
DR UniPathway; UPA00379; UER00550.
DR EvolutionaryTrace; Q5L084; -.
DR Proteomes; UP000001172; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Histidine metabolism; Lyase; NAD;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Urocanate hydratase"
FT /id="PRO_1000025128"
FT ACT_SITE 406
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 48..49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 172..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1X87"
FT BINDING 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1X87"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1X87"
FT BINDING 238..239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1X87"
FT BINDING 259..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1X87"
FT BINDING 269..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1X87"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1X87"
FT BINDING 488
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1X87"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 287..310
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 365..378
FT /evidence="ECO:0007829|PDB:1X87"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 479..488
FT /evidence="ECO:0007829|PDB:1X87"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:1X87"
FT STRAND 492..503
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 507..530
FT /evidence="ECO:0007829|PDB:1X87"
FT HELIX 534..543
FT /evidence="ECO:0007829|PDB:1X87"
SQ SEQUENCE 551 AA; 60008 MW; 68E9C8B53BB21E03 CRC64;
MAEKRTVSPP AGTERRAKGW IQEAALRMLN NNLHPDVAER PDELIVYGGI GKAARNWECY
EAIVDTLLRL ENDETLLIQS GKPVAVFRTH PDAPRVLIAN SNLVPAWATW DHFHELDKKG
LIMYGQMTAG SWIYIGSQGI VQGTYETFAE VARQHFGGTL AGTITLTAGL GGMGGAQPLA
VTMNGGVCLA IEVDPARIQR RIDTNYLDTM TDSLDAALEM AKQAKEEKKA LSIGLVGNAA
EVLPRLVEMG FVPDVLTDQT SAHDPLNGYI PAGLTLDEAA ELRARDPKQY IARAKQSIAA
HVRAMLAMQK QGAVTFDYGN NIRQVAKDEG VDDAFSFPGF VPAYIRPLFC EGKGPFRWVA
LSGDPEDIYK TDEVILREFS DNERLCHWIR MAQKRIKFQG LPARICWLGY GERAKFGKII
NDMVAKGELK APIVIGRDHL DSGSVASPNR ETEGMKDGSD AIADWPILNA LLNAVGGASW
VSVHHGGGVG MGYSIHAGMV IVADGTKEAE KRLERVLTTD PGLGVVRHAD AGYELAIRTA
KEKGIDMPML K
