ID A0A402CV22_9BACT Unreviewed; 686 AA.
AC A0A402CV22;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=CCAX7_23030 {ECO:0000313|EMBL:BDI30252.1}, CCAX7_23070
GN {ECO:0000313|EMBL:GCE53793.1};
OS Capsulimonas corticalis.
OC Bacteria; Armatimonadota; Armatimonadia; Capsulimonadales;
OC Capsulimonadaceae; Capsulimonas.
OX NCBI_TaxID=2219043 {ECO:0000313|EMBL:GCE53793.1};
RN [1] {ECO:0000313|EMBL:GCE53793.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:GCE53793.1};
RA Li J., Tonouchi A.;
RT "Draft Genome Sequence of Capsulimonas corticalis strain AX-7.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:BDI30252.1, ECO:0000313|Proteomes:UP000287394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI30252.1,
RC ECO:0000313|Proteomes:UP000287394};
RA Li J., Kudo C., Tonouchi A.;
RT "Capsulimonas corticalis gen. nov., sp. nov., an aerobic capsulated
RT bacterium, of a novel bacterial order, Capsulimonadales ord. nov., of the
RT class Armatimonadia of the phylum Armatimonadetes.";
RL Int. J. Syst. Evol. Microbiol. 69:220-226(2019).
RN [3] {ECO:0000313|EMBL:BDI30252.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI30252.1};
RA Li J., Tonouchi A.;
RL Submitted (MAY-2022) 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; AP025739; BDI30252.1; -; Genomic_DNA.
DR EMBL; BHFQ01000005; GCE53793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402CV22; -.
DR KEGG; ccot:CCAX7_23030; -.
DR InParanoid; A0A402CV22; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000287394; Chromosome.
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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Reference proteome {ECO:0000313|Proteomes:UP000287394}.
FT DOMAIN 15..392
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 403..614
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 630..685
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 686 AA; 78230 MW; 644EFE826B32A178 CRC64;
MEKALRVSHL TLGVCYYPEH WDESLWADDF RRMREMSLEV IRIGEFAWSI FEPEEGRFEF
GFFDRVMDLA HKHSLRVILG TPTATPPVWL TQKYPEALNA NRQGVVYQHG MRAHCNHTAP
IFRELSARIA SRMAEHYYKH PALWGWQIDN ELNCEVNVFY ADSDHAAFRV WLQEKYETLN
RLNAAWGAVF WNQTYSDWSQ VYLSRPTPAD SPNPHQALDE KRFISDSTIS YAKLQADAIR
AHDTTHFITT NGLFGHLDSH HLTDETLDFI SYDAYPLFSE ASLESSPEPM RDRRWGWNLS
AVRGISRRFC IMEQQSGPGG WVNRLELPSP KPGQVRLWTY QSIAHGADMV LFFRWRTATM
GTEIYWHGIN DYHNQANRRC AEVARIGQEL LRLADVAGSA YQADVAILRD YDNEWDGELD
TWHGPYERQS ASAWYAALQR RHVPVDSLTL RPGIRRREMS RYRVLIYPHP TILTDETARM
LKEYANAGGR IIFGCRTGYK DIHGQCPMRP FPGAVADLCG VTVEDFTRIG KYQTEPSLDW
DGVNAQFGEL KSGPFNDILR LENPEASVIA SYAADAGYYA GKPALTRNPW GDGVAYYYGG
VFTEPVANAL AEHLGLNSPL ADRLTLPRDI EAAIRAQPDG ETFVFLLNYA DTPRTIQAHS
EMVDLISGET VLGEVVMEPY GVLALR
//
