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BGAL_YERPN
ID   BGAL_YERPN              Reviewed;        1060 AA.
AC   Q1CI76; C4GTT5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01687};
DE            Short=Beta-gal {ECO:0000255|HAMAP-Rule:MF_01687};
DE            EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687};
DE   AltName: Full=Lactase {ECO:0000255|HAMAP-Rule:MF_01687};
GN   Name=lacZ {ECO:0000255|HAMAP-Rule:MF_01687}; OrderedLocusNames=YPN_1975;
GN   ORFNames=YP516_2199;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01687};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01687};
CC   -!- COFACTOR:
CC       Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC       Note=Binds 1 sodium ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01687};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01687}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01687}.
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DR   EMBL; CP000305; ABG18304.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000011; EEO76599.1; -; Genomic_DNA.
DR   RefSeq; WP_002214048.1; NZ_ACNQ01000011.1.
DR   AlphaFoldDB; Q1CI76; -.
DR   SMR; Q1CI76; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; ABG18304; ABG18304; YPN_1975.
DR   GeneID; 57976920; -.
DR   KEGG; ypn:YPN_1975; -.
DR   HOGENOM; CLU_002346_0_2_6; -.
DR   OMA; SNWQLQG; -.
DR   Proteomes; UP000008936; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   HAMAP; MF_01687; Beta_gal; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032312; LacZ_4.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF16353; DUF4981; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Magnesium; Metal-binding; Sodium.
FT   CHAIN           1..1060
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000367019"
FT   ACT_SITE        477
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   ACT_SITE        553
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         209
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         432
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         434
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         477
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         477
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         553..556
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         613
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         617
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         620
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         620
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         1035
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   SITE            373
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   SITE            407
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ   SEQUENCE   1060 AA;  122625 MW;  1142D7FC68E46697 CRC64;
     MTSQEKVPLQ VQLSLPQILS RRDWENPQIT QYHRLEAHPP FHSWRDVESA QKDRPSPQQQ
     TLNGLWSFSY FTQPEAVPEH WVRCDLAEAK PLPVPANWQL HGYDAPIYTN IQYPIPVNPP
     RVPDLNPTGC YSRDFTLEPS WLASGKTRII FDGVSSAFYL WCNGQWVGYS QDSRLPAEFD
     LTPYLQAGSN RIAVLVLRWS DGSYLEDQDM WRMSGIFRDV KLLHKPEIHL RDIHIMTHLS
     PEFTSANLEV MAAVNIPSLQ LNDPQVTGSY QLRVQLWLAD KLVASLQQPL GTQAIDERGP
     YTDRTQLVLR IDQPLLWSAE QPTLYRAVVS LLNHQQELIE AEAYDVGFRQ VAIHQGLLKI
     NGKAVLIRGV NRHEHHPQTG QAIDEESLLQ DILLMKQHNF NAVRCSHYPN HPLWYRLCDR
     YGLYVVDEAN IETHGMQPMS RLSDDPSWFS AFSERVTRMV QRDRNHPCII IWSLGNESGH
     GATHDALYRW IKTNDPTRPV QYEGGGANTL ATDILCPMYA RVDEDQPFPA VPKWSIKKWI
     GLPNESRPLI LCEYAHAMGN SFGGFARYWQ AFRQYPRLQG GFIWDWVDQS LTHHNDHGQP
     YWAYGGDFGD TPNDRQFCMN GLVFPDRSPH PSLYEAQCAQ QFFQFSLLST TPLVINITSE
     YLFRESDNEQ LYWRIMLEGE SVLEGSQPLN LSPESSQCYR LAEKLPTLNK PGQLWLNVEI
     RQPKETPWSP AQHRSAWHQW RLPQPLFSPS SDLTNATAHY APQLQHNLQL QHDLQLQQDE
     QHIKVTYQQQ CWQFSRQTGR LAQWWVADKP MLLRPLQDQF VRAPLDNDIG ISEATHIDPN
     AWVERWKKAG MYQLQQRCLS LHVDHLSHSV QISAEYGYEF EQEPLLHSHW VYRFDRHGRM
     TIDVNVRIAT SLPAPARIGM CCQLADISPT VEWLGLGPHE NYPDRQLAAQ YGHWSLPLEQ
     MHTAYIFPSE NGLRCNTHTL NYGRWTLTGD FHFGISRYST QQLMVTSHQH LLEPEEGTWL
     NIDGFHMGVG GDDSWSPSVH IDDILTRETY QYQICWQYKV
 
 
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