BGAL2_DICDI
ID BGAL2_DICDI Reviewed; 761 AA.
AC Q54MV6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Probable beta-galactosidase 2;
DE Short=Lactase 2;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=glb2; ORFNames=DDB_G0285637;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64656.1; -; Genomic_DNA.
DR RefSeq; XP_638187.1; XM_633095.1.
DR AlphaFoldDB; Q54MV6; -.
DR SMR; Q54MV6; -.
DR STRING; 44689.DDB0266381; -.
DR PaxDb; Q54MV6; -.
DR EnsemblProtists; EAL64656; EAL64656; DDB_G0285637.
DR GeneID; 8625233; -.
DR KEGG; ddi:DDB_G0285637; -.
DR dictyBase; DDB_G0285637; glb2.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q54MV6; -.
DR OMA; CGNYNHG; -.
DR PhylomeDB; Q54MV6; -.
DR PRO; PR:Q54MV6; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PF01301; Glyco_hydro_35; 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 Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..761
FT /note="Probable beta-galactosidase 2"
FT /id="PRO_0000328063"
FT ACT_SITE 195
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 761 AA; 87415 MW; 5220AD3C8EFB7627 CRC64;
MGTIKNNFQL LWLILLIVVL VNGKSINKNN NNNKNEIINV TYDGRSLIIN GERKLLFSGS
IHYPRTSEEM WPIILKQSKD AGIDIIDTYI FWNIHQPNSP SEYYFDGNAN ITKFLDLCKE
FDLYVNLRIG PYVCAEWTYG GFPIWLKEIP NIVYRDYNQQ WMNEMSIWME FVVKYLDNYF
APNGGPIILA QVENEYGWLE QEYGINGTEY AKWSIDFAKS LNIGIPWIMC QQNDIESAIN
TCNGYYCHDW ISSHWEQFPN QPSFWTENWI GWFENWGQAK PKRPVQDILY SNARFIAYGG
SLINYYMWFG GTNFGRTSGG PWIITSYDYD APLDEFGQPN EPKFSLSSKF HQVLHAIESD
LLNNQPPKSP TFLSQFIEVH QYGINLSFIT NYGTSTTPKI IQWMNQTYTI QPWSVLIIYN
NEILFDTSFI PPNTLFNNNT INNFKPINQN IIQSIFQISD FNLNSGGGGG DGDGNSVNSV
SPIEQLLITK DTSDYCWYST NVTTTSLSYN EKGNIFLTIT EFYDYVHIFI DNEYQGSAFS
PSLCQLQLNP INNSTTFQLQ ILSMTIGLEN YASHMENYTR GILGSILIGS QNLTNNQWLM
KSGLIGENIK IFNNDNTINW QTSPSSSSSS LIQKPLTWYK LNISLVGLPI DISSTVYALD
MSSMNKGMIW VNGYSIGRYW LIEATQSICN QSAIENYSYI GEYDPSNYRI DCNKPSQSIY
SVPIDWLFNN NYNNQYATII IIEELNGNPN EIQLLSNKII N
