ID C6WI75_ACTMD Unreviewed; 660 AA.
AC C6WI75;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Amir_2173 {ECO:0000313|EMBL:ACU36118.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU36118.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU36118.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
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; CP001630; ACU36118.1; -; Genomic_DNA.
DR RefSeq; WP_015801007.1; NC_013093.1.
DR AlphaFoldDB; C6WI75; -.
DR STRING; 446462.Amir_2173; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; ami:Amir_2173; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_11; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000002213; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:ACU36118.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ACU36118.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 16..381
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 392..584
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 594..658
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 660 AA; 71863 MW; B594E07E71793096 CRC64;
MGLGAAARGR LLYGGDYNPE QWPEEVWAED VELMKRAGVN VATVGVFSWA TIEPEPGARE
FGWLDRVLSL LHANGIAVCL ATPTASPPPW LGHRHPETLP VDFDGRRLSY GSRNQFCPSS
PVYRKRSLEL VTDLAARYAH HPAVVMWHVN NEYCEVCHCD VSAEHFRRWL RARHGTLDAL
NAAWSTAFWS QRYGDWDEVV PPRRAPYLIN PAQRLDFARF SSDALLECFL AEKAVLRAAN
PDVPITTNFM GLDQPMDYWS LAAHEDVVSH DWYPDPSDPK SHVGTAIAYD LVRSLAGGPW
ALMEQAASAV NWRHRNPAKP AGQLRAQSAQ AVARGADAVC FFQWRASAGG AEKFHSGMLP
HAGPDTRVFR EVCELGADLA RLEEVVGADV RASVAFALDW ESWWACRLDA HPAGDFDLLA
RVRDFYEPLF DLGVAVDFVR PDADLSGYAL VVVPNLYLLR DASRFESFVD GGGTLLVGFF
SGVVDGNDRI HPGGAPGPLR ELLGLTVHEM APVERELRCE SELLGEFTAD FWLDDVAPHG
AEVIARAGDA PVVLRHGRAW YTATRPEPAA TARLLAHLVE SAGVPRALPE LPSGVEAVRR
GGFLFLVNHN DDPVTVTVPG GGVDLLAGAG TGAGGGQGAE AAPADEVELG RFGVAVLRQP
//
