ID H9UBS1_FERPD Unreviewed; 614 AA.
AC H9UBS1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=Ferpe_0848 {ECO:0000313|EMBL:AFG34964.1};
OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG34964.1, ECO:0000313|Proteomes:UP000007384};
RN [1] {ECO:0000313|Proteomes:UP000007384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL Submitted (MAR-2012) 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; CP003260; AFG34964.1; -; Genomic_DNA.
DR RefSeq; WP_014451407.1; NC_017095.1.
DR AlphaFoldDB; H9UBS1; -.
DR STRING; 771875.Ferpe_0848; -.
DR KEGG; fpe:Ferpe_0848; -.
DR PATRIC; fig|771875.3.peg.872; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_0_0; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000007384; 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:0005975; P:carbohydrate 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 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; 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; 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}.
FT DOMAIN 7..367
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 379..562
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 614 AA; 72612 MW; 998C2B23E6119741 CRC64;
MDIYGADYYP EHWDRSFWKK HVDLMKVYGI EWVRIGEFMW SVVEPRNGEF DFSLLDEAIE
LLSENGIKII LGTPTATPPA WLVSKYPEIL PVDWNGRVRG FGSRRHYSPN SKAYLEYALR
IVEQYASRYG DAIDVWQIDN EFGCHGTTYS FTNEDLVAFR EWLKEKYGTI ENLNKHWGTV
FWSQTYNSWD EIVFPINTPT FENPHQMLDI YRFMSDSFIR FLKSQVEIIR KYSSKPITHN
FMVDFMDLDY RRMARYVDFV SWDNYIATEE YDPLRQSANH SLMRSLKHQP FLVIEQQPAR
VNWRQVNENY EPEYLAMWTK QAYLNGAMGV MPFRFDQIRF GAEQYHAGLL DYYGRPTKRL
EAYSKVKNQT PGVITPKPEV AIYFDYENEW IHRINHLNRN FKYWDAIVDI YKAVKNLGYN
AEFVFNEDEV EGYNVLIVPY ASYISEEFIE KIKKFEGPVY LTAMSSIKDK YNWLTERMPW
HLVDEFGIEV VDFGGIKEEK GYLFSQCVTT LFWKDELEVL DAKVIGSFEN GAPLVTVKNN
RYYVASVLDE NGWKLLLSEN LRPRVLGKGY ELVNVERDSR ELTGVLNTLP TENKLYIDGS
LHVLKPFEFR FVER
//
