HUTU_PSEPU
ID HUTU_PSEPU Reviewed; 557 AA.
AC P25080;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Urocanate hydratase {ECO:0000255|HAMAP-Rule:MF_00577};
DE Short=Urocanase {ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000303|PubMed:1677899};
DE EC=4.2.1.49 {ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000269|PubMed:7901006};
DE AltName: Full=Imidazolonepropionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00577};
GN Name=hutU {ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000303|PubMed:1677899};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-23.
RC STRAIN=NIC II;
RX PubMed=1677899; DOI=10.1016/0014-5793(91)80938-y;
RA Fessemaier M., Frank R., Retey J., Schubert C.;
RT "Cloning and sequencing the urocanase gene (hutU) from Pseudomonas
RT putida.";
RL FEBS Lett. 286:55-57(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC
RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90;
RA Allison S.L., Phillips A.T.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, MASS SPECTROMETRY, MUTAGENESIS OF CYS-64; CYS-192; CYS-198;
RP CYS-355; CYS-411 AND CYS-544, AND ACTIVE SITE.
RC STRAIN=NIC II;
RX PubMed=7901006; DOI=10.1111/j.1432-1033.1993.tb18262.x;
RA Lenz M., Retey J.;
RT "Cloning, expression and mutational analysis of the urocanase gene (hutU)
RT from Pseudomonas putida.";
RL Eur. J. Biochem. 217:429-434(1993).
RN [4] {ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL, ECO:0007744|PDB:1W1U}
RP X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) IN COMPLEX WITH NAD, AND COFACTOR.
RX PubMed=15313616; DOI=10.1016/j.jmb.2004.07.028;
RA Kessler D., Retey J., Schulz G.E.;
RT "Structure and action of urocanase.";
RL J. Mol. Biol. 342:183-194(2004).
RN [5] {ECO:0007744|PDB:2V7G}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NAD, AND COFACTOR.
RX PubMed=18187656; DOI=10.1126/science.1150421;
RA Grueninger D., Treiber N., Ziegler M.O., Koetter J.W., Schulze M.S.,
RA Schulz G.E.;
RT "Designed protein-protein association.";
RL Science 319:206-209(2008).
CC -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5-
CC propionate. {ECO:0000255|HAMAP-Rule:MF_00577,
CC ECO:0000269|PubMed:7901006}.
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, ECO:0000269|PubMed:7901006};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00577,
CC ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
CC ECO:0000269|PubMed:7901006};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00577,
CC ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35.4 uM for urucanate {ECO:0000269|PubMed:7901006};
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7901006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00577}.
CC -!- MASS SPECTROMETRY: Mass=60686; Mass_error=15; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7901006};
CC -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000255|HAMAP-
CC Rule:MF_00577, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X58483; CAA41392.1; -; Genomic_DNA.
DR EMBL; M33923; AAA50311.1; -; Genomic_DNA.
DR PIR; S17184; DWPSUP.
DR PIR; T45008; T45008.
DR PDB; 1UWK; X-ray; 1.19 A; A/B=1-557.
DR PDB; 1UWL; X-ray; 1.76 A; A/B=1-557.
DR PDB; 1W1U; X-ray; 2.23 A; A/B=2-557.
DR PDB; 2V7G; X-ray; 2.00 A; A/B/C/D=2-557.
DR PDBsum; 1UWK; -.
DR PDBsum; 1UWL; -.
DR PDBsum; 1W1U; -.
DR PDBsum; 2V7G; -.
DR AlphaFoldDB; P25080; -.
DR SMR; P25080; -.
DR STRING; 1240350.AMZE01000145_gene577; -.
DR eggNOG; COG2987; Bacteria.
DR BioCyc; MetaCyc:MON-11616; -.
DR BRENDA; 4.2.1.49; 5092.
DR UniPathway; UPA00379; UER00550.
DR EvolutionaryTrace; P25080; -.
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; Direct protein sequencing; Histidine metabolism;
KW Lyase; NAD.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1677899"
FT CHAIN 2..557
FT /note="Urocanate hydratase"
FT /id="PRO_0000207344"
FT ACT_SITE 411
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000305|PubMed:7901006"
FT BINDING 53..54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
FT ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL,
FT ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G"
FT BINDING 131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
FT ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL,
FT ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G"
FT BINDING 177..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
FT ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL,
FT ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G"
FT BINDING 197..202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15313616,
FT ECO:0000269|PubMed:18187656, ECO:0007744|PDB:1UWK,
FT ECO:0007744|PDB:1UWL, ECO:0007744|PDB:1W1U,
FT ECO:0007744|PDB:2V7G"
FT BINDING 243..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
FT ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL,
FT ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G"
FT BINDING 264..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
FT ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL,
FT ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G"
FT BINDING 274..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
FT ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL,
FT ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G"
FT BINDING 323..324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15313616,
FT ECO:0000269|PubMed:18187656, ECO:0007744|PDB:1UWK,
FT ECO:0007744|PDB:1UWL, ECO:0007744|PDB:2V7G"
FT BINDING 455..456
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15313616,
FT ECO:0000269|PubMed:18187656, ECO:0007744|PDB:1W1U,
FT ECO:0007744|PDB:2V7G"
FT BINDING 493
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656,
FT ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL,
FT ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G"
FT MUTAGEN 64
FT /note="C->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:7901006"
FT MUTAGEN 192
FT /note="C->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:7901006"
FT MUTAGEN 198
FT /note="C->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:7901006"
FT MUTAGEN 355
FT /note="C->A: Minor loss in activity."
FT /evidence="ECO:0000269|PubMed:7901006"
FT MUTAGEN 411
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7901006"
FT MUTAGEN 544
FT /note="C->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:7901006"
FT CONFLICT 164..167
FT /note="TVKA -> SLKG (in Ref. 2; AAA50311)"
FT /evidence="ECO:0000305"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 131..137
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 292..315
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 370..383
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 453..459
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 469..481
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 484..491
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:1UWK"
FT STRAND 500..508
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 512..535
FT /evidence="ECO:0007829|PDB:1UWK"
FT HELIX 539..547
FT /evidence="ECO:0007829|PDB:1UWK"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:1UWK"
SQ SEQUENCE 557 AA; 60804 MW; 5AFD1E3307F34434 CRC64;
MTDNNKYRDV EIRAPRGNKL TAKSWLTEAP LRMLMNNLDP QVAENPKELV VYGGIGRAAR
NWECYDKIVE TLTRLEDDET LLVQSGKPVG VFKTHSNAPR VLIANSNLVP HWANWEHFNE
LDAKGLAMYG QMTAGSWIYI GSQGIVQGTY ETFVEAGRQH YGGTVKAKWV LTAGLGGMGG
AQPLAATLAG ACSLNIECQQ SRIDFRLETR YVDEQATDLD DALVRIAKYT AEGKAISIAL
HGNAAEILPE LVKRGVRPDM VTDQTSAHDP LNGYLPAGWT WEQYRDRAQT EPAAVVKAAK
QSMAVHVQAM LDFQKQGVPT FDYGNNIRQM AKEEGVANAF DFPGFVPAYI RPLFCRGVGP
FRWAALSGEA EDIYKTDAKV KELIPDDAHL HRWLDMARER ISFQGLPARI CWVGLGLRAK
LGLAFNEMVR SGELSAPVVI GRDHLDSGSV SSPNRETEAM RDGSDAVSDW PLLNALLNTA
GGATWVSLHH GGGVGMGFSQ HSGMVIVCDG TDEAAERIAR VLTNDPGTGV MRHADAGYDI
AIDCAKEQGL DLPMITG
