ID D2RZ19_HALTV Unreviewed; 972 AA.
AC D2RZ19;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN OrderedLocusNames=Htur_3122 {ECO:0000313|EMBL:ADB61987.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB61987.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB61987.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP001860; ADB61987.1; -; Genomic_DNA.
DR AlphaFoldDB; D2RZ19; -.
DR STRING; 543526.Htur_3122; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; htu:Htur_3122; -.
DR eggNOG; arCOG07337; Archaea.
DR HOGENOM; CLU_009998_0_0_2; -.
DR Proteomes; UP000001903; 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; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
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; IPR006311; TAT_signal.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ADB61987.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADB61987.1}.
FT DOMAIN 65..210
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 212..319
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 321..595
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT REGION 33..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 107572 MW; 6C52CDFD2ED6221C CRC64;
MDRDSHEEDR RTVPISRRTL LSSVPGAAIG AALPIGTASA RDDGDDESLG RLTPRPATTG
DGDVRSLNGT WEFALSTTID DQGAEWREAE VPGQWGYSES AIPEGPAEWY PPEGQLGWYR
REFEAPKSDR ERLLLRFDAV YSEARVYLNG AEIGHHVGGY TPFEIDVTDH VEAGTNVLSV
GVAQASPADD MAWQNVTGGI TRDVTLVSVP EIHIADYDVR THLQGSSATV DVETRIENAS
GADADATLEV TLSDPNGETV ATTERSLSSR EGGSCDPSTT LEVADPNTWN PEEPQLYTLE
IDLNAGDSTE RVTQRLGIRE IEVVGDELRL NGEAVTLRGV NWEEIHIPDH GHAVPPELTR
EDARRLKEAN VNYVRTAHHP TSEAFLDACD ELGLVVEVEA PHTFVGRGRG DPYPEIVVSQ
TVEMVERDKN RTSVCLWSIA NESEWYDAFE TAGRLTKAID PTRPTIFNYD NYDPDDPWHD
VYDVRSQHYP AFRADSTIEE YLGLDDPILF DEYAHTYCYN GRELVTDPGL RDQWGIPFER
IWERCRAGDS VAGGAIWAGG DHLERWRGYL WGLLDRHRRP RPEYWHVKKI YSPVRVVETE
WLGNGNVLRL TIENRHEFVD LADRSIEFEG ARNSGNRPIE AAPGERVTVT VPVAEDRLEL
RVTHPHGHTI EQAVFTVDSP GCESYPVPTG TPLEIDEESV RTTEGPPMSV DRNTGRVEVQ
PEDGQGTPVV VGGPELVLTP TEAEASQEGS GAIDHRPDGR TVTDVRVVED GAAVAIDVEY
AVATGTFVLR PVDGGVEVEY EFEIEEALDV REVGVALPLT RDLTTLSWRR EGQWSTYPDD
HIGRTEGTAV AFPEGTRPDH EEIRLGSDRP WKDDATSHGS NDFRGTKRNV YTAALVNDHG
AGVQLRSEGD HHVRAQVRSE SVDLLALERS LSGTNPFGWM NRQPVLNEDP TIEADEIVRG
NAAFEIRGSP SV
//
