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Database: UniProt
Entry: A0A1H5MC92_9MICO
LinkDB: A0A1H5MC92_9MICO
Original site: A0A1H5MC92_9MICO 
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
//
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