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HUTU_BRUSI
ID   HUTU_BRUSI              Reviewed;         557 AA.
AC   A9WVU5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BSUIS_B0925;
OS   Brucella suis (strain ATCC 23445 / NCTC 10510).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=470137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23445 / NCTC 10510;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00577}.
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DR   EMBL; CP000912; ABY39881.1; -; Genomic_DNA.
DR   RefSeq; WP_006199088.1; NC_010167.1.
DR   AlphaFoldDB; A9WVU5; -.
DR   SMR; A9WVU5; -.
DR   EnsemblBacteria; ABY39881; ABY39881; BSUIS_B0925.
DR   KEGG; bmt:BSUIS_B0925; -.
DR   HOGENOM; CLU_018868_0_1_5; -.
DR   OMA; LVGDWAN; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000008545; Chromosome II.
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   3: Inferred from homology;
KW   Cytoplasm; Histidine metabolism; Lyase; NAD.
FT   CHAIN           1..557
FT                   /note="Urocanate hydratase"
FT                   /id="PRO_1000082348"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         52..53
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         176..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         242..243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         263..267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         273..274
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         322
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         492
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
SQ   SEQUENCE   557 AA;  61272 MW;  32C04DED715A339F CRC64;
     MSNPRHNERE VRSPRGDELN AKSWLTEAPL RMLMNNLDPD VAERPHELVV YGGIGRAART
     WDDFDRIVAT LKTLNDDETL LVQSGKPVGV FRTHKDAPRV LIANSNLVPH WANWDHFNEL
     DKKDLAMYGQ MTAGSWIYIG AQGIVQGTYE TFVEAGRQHY GGNLKGRWIL TGGLGGMGGA
     QPLAAVMAGA CCLAVECDET RADFRLRTRY VDEKTHSLDE ALAKIDAWTK AGEAKSIALI
     GNAAEIFPEL VKRGVKPDIV TDQTSAHDPV HGYLPLGWTV AEWRAKQEND PKAVEKAARA
     SMKVQVQAML DFWNAGIPTV DYGNNIRQMA LEEGLENAFA FPGFVPAYIR PLFCRGIGPF
     RWAALSGDPE DIAKTDAKVK ELLPDNKHLH NWLDMAKERI AFQGLPARIC WVGLGDRHRL
     GLAFNEMVRN GELKAPIVIG RDHLDSGSVA SPNRETEAMK DGSDAVSDWP LLNALLNTAS
     GATWVSLHHG GGVGMGFSQH AGMVICCDGT EDADRRLERV LWNDPATGVM RHADAGYDIA
     LDWARKQGLR LPAILGN
 
 
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