ID A0A1H5MC92_9MICO Unreviewed; 692 AA.
AC A0A1H5MC92;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN ORFNames=SAMN04488554_3239 {ECO:0000313|EMBL:SEE86068.1};
OS Ruania alba.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae; Ruania.
OX NCBI_TaxID=648782 {ECO:0000313|EMBL:SEE86068.1, ECO:0000313|Proteomes:UP000199220};
RN [1] {ECO:0000313|Proteomes:UP000199220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21368 {ECO:0000313|Proteomes:UP000199220};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 ECO:0000256|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR EMBL; FNTX01000002; SEE86068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5MC92; -.
DR STRING; 648782.SAMN04488554_3239; -.
DR Proteomes; UP000199220; Unassembled WGS sequence.
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:SF1; BETA-GALACTOSIDASE GANA; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Reference proteome {ECO:0000313|Proteomes:UP000199220}.
FT DOMAIN 39..410
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 421..622
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 631..689
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 692 AA; 75935 MW; 5E7DBBC13FA5939B CRC64;
MNTLGRMADD VTAPEPTTPA KPAIPSWPIG LTVMGYGGDY NPEQWPMEVR LEDIAMMREA
GVNLVSLAIF SWATLEPREG RYDWTWLDNI LDRLQAAGVK VALATATASP PPWLTANHPE
ILPRTAEGVE LHQGGRQSYA PSSPVYREYA VKMAKAIAER YAEHPALALW HIDNEIGCHV
PHDYSESAQR AFRTWLRRRY RTIDRLNTAW GTAFWSQRYS AFKDVLPPLS APTYANPTQQ
LDFARFSSDT LLDYYKKLRD AVRPITPHIP STTNFMVNLS TKWMDYYRWA REVDVVATDH
YTIAADAERE VDLALAADMT RGVAGGKPWI LMEHSTGAVN WQPRNRAKGP GEMLRNSLAH
VARGADSVMF FQFRQSQAGA EKFHSALVPH AGRESAIWRE SVHLGEVLAN LGDVVGSRVQ
ARVALLFDYQ AWWACELDSH PSEDVTYGDR LRALYRELWR RGVATDVVQP GADLSEYDLI
LVPTLYLITD ADAANVAAAA ERGATVLITY FSGIVDENDH ARLGGYPGAF RELLGVRTDE
FFPLLADERV TLDDGTTADV WTERVEVTTA EVVRSFTDGP LPDGPAVTRN AVGEGAAWYV
ATRQDEAGTA AVIEQVLAES GVAPAAATTP GVEVVRRAEH GEDGGNRSFL FVLNHTDAAA
TVPATGTDLV SGAEVGESVV VPAHGVAVVA EG
//