ID M0JQH3_9EURY Unreviewed; 664 AA.
AC M0JQH3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=C436_16220 {ECO:0000313|EMBL:EMA11246.1}, KDQ40_16275
GN {ECO:0000313|EMBL:QUJ73783.1};
OS Haloarcula sinaiiensis ATCC 33800.
OG Plasmid pHsi117 {ECO:0000313|EMBL:QUJ73783.1,
OG ECO:0000313|Proteomes:UP000682967}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA11246.1, ECO:0000313|Proteomes:UP000011659};
RN [1] {ECO:0000313|EMBL:EMA11246.1, ECO:0000313|Proteomes:UP000011659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA11246.1,
RC ECO:0000313|Proteomes:UP000011659};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [2] {ECO:0000313|EMBL:QUJ73783.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ73783.1};
RC PLASMID=pHsi117 {ECO:0000313|EMBL:QUJ73783.1};
RA Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT Haloarcula sinaiiensis.";
RL Submitted (APR-2021) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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DR EMBL; AOLR01000029; EMA11246.1; -; Genomic_DNA.
DR EMBL; CP073367; QUJ73783.1; -; Genomic_DNA.
DR RefSeq; WP_004965344.1; NZ_CP073367.1.
DR AlphaFoldDB; M0JQH3; -.
DR GeneID; 64824545; -.
DR KEGG; hsin:KDQ40_16275; -.
DR PATRIC; fig|662476.7.peg.3246; -.
DR OrthoDB; 85141at2157; -.
DR Proteomes; UP000011659; Unassembled WGS sequence.
DR Proteomes; UP000682967; Plasmid pHsi117.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Plasmid {ECO:0000313|EMBL:QUJ73783.1}.
FT DOMAIN 6..388
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 397..600
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 610..654
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT REGION 273..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 75128 MW; 05E27BC550351D5E CRC64;
MTVGVCYFPE HWSRERWAQD VEQMVEAGIE YVRMGEFSWS RIEPEPGDID LSWLEDAVSL
IGDHGMRTIL CTPTATPPKW LIDQHPSILQ EEPDGTPRHY GSRRHYCFNS PAYRDETHRI
VSMMAERFAD NPHVVGWQTD NEYGCHETIR CWCNDCARAF REWLREKYDD INSLNEAWGT
SFWSQRLRSF EEVDPPRHTA AEHHPSRLLD YYRFSAESAV EYNAIHTERL RAVNDDWFIT
HNFMGDFNSC DVYGFTEDLD LITWDSYPTG FAQDRRPDAA SPDELRAGDP DQVGMNHDLY
RGAKQQPFWV MEQQPGDVNW PPYAPQPGEG AMRLWAHHAV AHGADTVVYF RWRRCREGQE
QYHAGLRKQD GSPDRGYHDA DKAATELGEL DLGPVDADVA VLHDYDNLWA TSIQPHAPDW
EYWTHMRQYY RALRSRSVQV DVVHPDWDLS GYDAIIAPAL HLVSEDLAKT LKSEVESGTE
LLITVRSGAK DQYNKLPDTS APGPLADIVG ATVDQHESVP EELDRTVTYD GETYSYRTFA
EWLDPDEASV VGSHIGGVGD GYAAITENEV GAGHVAYCGI WPEADLADSV VSDLLDRAGI
SRTERFPTGV RAAERDGYTW VTNFTSDPVS VTPPADARWL VGDNTVGAFG AVVYEGVASN
LSLK
//
