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BGAL_AERHH
ID   BGAL_AERHH              Reviewed;        1025 AA.
AC   A0KQH4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=AHA_4101;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK36888.1; -; Genomic_DNA.
DR   RefSeq; WP_011707763.1; NC_008570.1.
DR   RefSeq; YP_858525.1; NC_008570.1.
DR   AlphaFoldDB; A0KQH4; -.
DR   SMR; A0KQH4; -.
DR   STRING; 380703.AHA_4101; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; ABK36888; ABK36888; AHA_4101.
DR   KEGG; aha:AHA_4101; -.
DR   PATRIC; fig|380703.7.peg.4057; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_0_2_6; -.
DR   OMA; SNWQLQG; -.
DR   Proteomes; UP000000756; 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; 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.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW   Sodium.
FT   CHAIN           1..1025
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000366979"
FT   ACT_SITE        462
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   ACT_SITE        538
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         204
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         417
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         419
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         462
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         538..541
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         598
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         602
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         605
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         605
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   BINDING         1003
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   SITE            358
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT   SITE            392
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ   SEQUENCE   1025 AA;  115234 MW;  9358E7C1D095FAD1 CRC64;
     MLREIVARQD WQTQAITAVN RLPAHTPLFS WRSEAAARDD LASPSRTLLD GEWRFSFFEA
     PELVPEHWLV EDLPDACAIK VPGNWQLDAA YPGLRLATDV PIYTNIKYPF PCDPPRVPAE
     NPTGCYSREF SVPADWLASG QTRIIFDGVD SAFHLFCNGR WVGYSQDSRL PAEFDLTSFL
     CGGDNRLAVL VLRWSDGSYL EDQDMWRMSG IFRSVSLLHK PVRHLMDIRV TPELDACYRD
     GRLKIALQAA NGAGLSVAAC LYDGGERVAT LRQPIGTQAI DEKGAYDDRA ECWLEVAAPR
     KWSAETPHLY RLTLTLLDEQ GEPIESEAYD VGFRAVEIRG GLLRVNGQPL LIRGANRHEH
     DVASGHVVTP AAIEQDLLLM KRHNFNSVRC SHYPNHPELY RLCDRLGLYV VDEANLETHG
     MTPMGRLARD PAWSNAFLER VTRMVARDFN HPSIIIWSLG NESGYGPAHD AMYGWVKRAD
     PSRPVQYEGG GADTPATDII CPMYARTHQD QPFPAVPKWA LAKWIGLPGE TRPLILCEYA
     HAMGNSLGGY AHYWQAFRDH PRLQGGFVWD WVDQGLDKLT DDGRHFWAYG GDFGDTPNDR
     QFCCNGLVFP DRTPHPALFE ARRAQQPFGL TLLERQPLTV EIRSEYLFRE TDNERLQWRL
     CEDGVVVSQG ECPLTLAPQG SMMLTLLERL PAFAPGALAW LDLAIVQPAA TPWSAVGHEV
     ARQQCMLPAP LSLPVARTPA TFIELADGWQ IRAAASEWRL DKASGRVQSW CKLGREQLKE
     AIADHFYRAP LDNDIGTSEA DHADPNAWIA RWQEAGLNEL QHRCLDMVVS PDQGVVTVHH
     GYFVGDALKL LTRWRHEFDQ DGAMRLAIEV QVAAEMPSLP RIGARLWLTD EVLATGEEVS
     WLGRGPHENY PDRLLAADLG RWQSPLDVLH TAYVFPTDNG LRCDTRQLQL GSIEVEGLFH
     FSLSRFSQQQ LAQARHQTDL VAEGGLHLCL DGFHMGIGGD DSWSQSVRPE YWLQPGGYYW
     NCVLR
 
 
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