HUTU_BACSU
ID HUTU_BACSU Reviewed; 552 AA.
AC P25503;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Urocanate hydratase {ECO:0000255|HAMAP-Rule:MF_00577};
DE Short=Urocanase {ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000303|PubMed:4990470};
DE EC=4.2.1.49 {ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000269|PubMed:4990470};
DE AltName: Full=Imidazolonepropionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00577};
GN Name=hutU {ECO:0000255|HAMAP-Rule:MF_00577}; OrderedLocusNames=BSU39360;
GN ORFNames=EE57A;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7704263; DOI=10.1099/13500872-141-2-337;
RA Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.;
RT "Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome
RT containing the hut and wapA loci.";
RL Microbiology 141:337-343(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-240.
RX PubMed=2454913; DOI=10.1128/jb.170.7.3199-3205.1988;
RA Oda M., Sugishita A., Furukawa K.;
RT "Cloning and nucleotide sequences of histidase and regulatory genes in the
RT Bacillus subtilis hut operon and positive regulation of the operon.";
RL J. Bacteriol. 170:3199-3205(1988).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=4990470; DOI=10.1016/s0021-9258(18)62959-x;
RA Kaminskas E., Kimhi Y., Magasanik B.;
RT "Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus
RT subtilis, two enzymes of the histidine degradation pathway.";
RL J. Biol. Chem. 245:3536-3544(1970).
RN [5] {ECO:0007744|PDB:2FKN}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD, AND COFACTOR.
RA Yu Y.-M., Liang Y.-H., Su X.-D.;
RT "Crystal structure of urocanase from Bacillus subtilis.";
RL Submitted (JAN-2006) 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 ECO:0000269|PubMed:4990470}.
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:4990470};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000269|Ref.5};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00577,
CC ECO:0000269|Ref.5};
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, ECO:0000269|PubMed:4990470}.
CC -!- SUBUNIT: Composed of at least two subunits.
CC {ECO:0000269|PubMed:4990470}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00577}.
CC -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000255|HAMAP-
CC Rule:MF_00577, ECO:0000305}.
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DR EMBL; D31856; BAA06643.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15972.1; -; Genomic_DNA.
DR EMBL; M20659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G69643; G69643.
DR RefSeq; NP_391815.1; NC_000964.3.
DR RefSeq; WP_003243634.1; NZ_JNCM01000034.1.
DR PDB; 2FKN; X-ray; 2.20 A; A/B/C/D=1-552.
DR PDBsum; 2FKN; -.
DR AlphaFoldDB; P25503; -.
DR SMR; P25503; -.
DR STRING; 224308.BSU39360; -.
DR PaxDb; P25503; -.
DR PRIDE; P25503; -.
DR EnsemblBacteria; CAB15972; CAB15972; BSU_39360.
DR GeneID; 937542; -.
DR KEGG; bsu:BSU39360; -.
DR PATRIC; fig|224308.179.peg.4261; -.
DR eggNOG; COG2987; Bacteria.
DR InParanoid; P25503; -.
DR OMA; LVGDWAN; -.
DR PhylomeDB; P25503; -.
DR BioCyc; BSUB:BSU39360-MON; -.
DR BioCyc; MetaCyc:HUTUBACSU-MON; -.
DR UniPathway; UPA00379; UER00550.
DR EvolutionaryTrace; P25503; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016153; F:urocanate hydratase activity; IBA:GO_Central.
DR GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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..552
FT /note="Urocanate hydratase"
FT /id="PRO_0000207334"
FT ACT_SITE 407
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 49..50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 173..175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 239..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 260..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 270..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT BINDING 489
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:2FKN"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 127..133
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 288..312
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 366..379
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 384..396
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 413..427
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 449..455
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:2FKN"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:2FKN"
FT STRAND 496..504
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 508..532
FT /evidence="ECO:0007829|PDB:2FKN"
FT HELIX 535..543
FT /evidence="ECO:0007829|PDB:2FKN"
SQ SEQUENCE 552 AA; 60600 MW; 70387718C975539F CRC64;
MTDVKKSIRA NRGTELECLG WEQEAVLRML RNNLDPEVAE KPEDLIVYGG IGKAARDWDA
FHAIEHSLKT LKNDETLLVQ SGKPVGMFRT HPQAPRVLLA NSVLVPKWAD WEHFHELEKK
GLMMYGQMTA GSWIYIGSQG ILQGTYETFA ELARQHFGGS LKGTLTLTAG LGGMGGAQPL
SVTMNEGVVI AVEVDEKRID KRIETKYCDR KTASIEEALA WAEEAKLAGK PLSIALLGNA
AEVHHTLLNR GVKIDIVTDQ TSAHDPLIGY VPEGYSLDEA DRLRQDTPEL YVRLAKQSMK
KHVEAMLAFQ QKGSIVFDYG NNIRQVAKDE GLENAFDFPG FVPAYIRPLF CEGKGPFRWA
ALSGDPADIY RTDALLKELF PTNKALHRWI DMAQEKVTFQ GLPSRICWLG YGERKKMGLA
INELVRTGEL KAPVVIGRDH LDCGSVASPN RETEAMKDGS DAVGDWAVLN ALVNTAAGAS
WVSFHHGGGV GMGYSLHAGM VAVADGSELA DERLARVLTS DPGMGIIRHA DAGYERAVEV
AKEQDIIVPM QK
