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Database: UniProt
Entry: C1F148_ACIC5
LinkDB: C1F148_ACIC5
Original site: C1F148_ACIC5 
ID   C1F148_ACIC5            Unreviewed;       664 AA.
AC   C1F148;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 56.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   OrderedLocusNames=ACP_0552 {ECO:0000313|EMBL:ACO31564.1};
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 /
OS   NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO31564.1, ECO:0000313|Proteomes:UP000002207};
RN   [1] {ECO:0000313|EMBL:ACO31564.1, ECO:0000313|Proteomes:UP000002207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 /
RC   161 {ECO:0000313|Proteomes:UP000002207};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B.,
RA   Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J.,
RA   Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D.,
RA   Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C.,
RA   Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S.,
RA   Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C.,
RA   Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D.,
RA   Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L.,
RA   Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; CP001472; ACO31564.1; -; Genomic_DNA.
DR   RefSeq; WP_012680939.1; NC_012483.1.
DR   ProteinModelPortal; C1F148; -.
DR   STRING; 240015.ACP_0552; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   EnsemblBacteria; ACO31564; ACO31564; ACP_0552.
DR   KEGG; aca:ACP_0552; -.
DR   eggNOG; ENOG4105D57; Bacteria.
DR   eggNOG; COG1874; LUCA.
DR   HOGENOM; HOG000221607; -.
DR   KO; K12308; -.
DR   OMA; GWGKGIV; -.
DR   OrthoDB; 831762at2; -.
DR   BioCyc; ACAP240015:G1GV4-536-MONOMER; -.
DR   Proteomes; UP000002207; Chromosome.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002207};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000313|EMBL:ACO31564.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002207}.
FT   DOMAIN       36    353       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      529    604       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    186    186       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    262    262       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   664 AA;  73454 MW;  A980E76B79C3D3C0 CRC64;
     MLALFLLPVS VMAAARRGNS SALSDQRGSF RVENGKFVLD GQPFQIISGE MHYERIPRAY
     WKARLQMAKA MGLNTIATYV FWNLHEPEPG KFDFSGNADL AQFIRDAQQT GLKVLLRAGP
     YSCAEWEFGG FPAWLMKNPK MQTALRSNDP EFMKPAEQWI LRLGREVAPL QVGYGGPIIG
     VQIENEYGDF GGDAAYLEHL KKIFLKAGFT QSLLYTANPS RALVRGSIPG VYSAVNFAPG
     HAAQALDSLA QLRAGQPLLS SEYWTGWFDH WGEPHQSKPL SLQVKDFNYI LRHGAGVNLY
     MFHGGTSFGM MSGSSWTKHQ FLPDVTSYDY GAPLDEAGHP TPAYYAYRKI IAAYLGHALP
     PVPAAPPVMA IAPFALHEAS SLWRGLPKPV VTKNPEPMEW LGQSYGFILY RKTLHHAVDG
     DLVLNGMNDY ALVYLNGKLQ GTLNRTCNDS TLMLHSNSAK TRLDILVENS GRINSTRMML
     HANKGLMGPV MLAGRALHGW KTYRLPMKPD TIADPLGMPQ ETHFNEKSTP AQAMSGPAFY
     RGTFRVETKS KQIPDTFLDI RGLGKGAVWI DGHPIGRYWN VGPQDTLYVP GPWLHRGKNE
     IMVLDLFQRT NLPRLAGLTQ PILNGPARKV CNATELSSAP AEMHGRGKGR AAQPGVSRAK
     ETKH
//
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