ID D8IW01_HERSS Unreviewed; 658 AA.
AC D8IW01;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 Name=lacA {ECO:0000313|EMBL:ADJ61799.1};
GN OrderedLocusNames=Hsero_0273 {ECO:0000313|EMBL:ADJ61799.1};
OS Herbaspirillum seropedicae (strain SmR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ61799.1, ECO:0000313|Proteomes:UP000000329};
RN [1] {ECO:0000313|EMBL:ADJ61799.1, ECO:0000313|Proteomes:UP000000329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ61799.1,
RC ECO:0000313|Proteomes:UP000000329};
RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA Weiss V.A., Yates M.A., Souza E.M.;
RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT fixing, plant-growth promoting beta-Proteobacteria.";
RL Submitted (APR-2010) 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; CP002039; ADJ61799.1; -; Genomic_DNA.
DR RefSeq; WP_013232321.1; NC_014323.1.
DR AlphaFoldDB; D8IW01; -.
DR STRING; 757424.Hsero_0273; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; hse:Hsero_0273; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_0_4; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000000329; 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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ADJ61799.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ADJ61799.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000329}.
FT DOMAIN 8..390
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 406..599
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 607..653
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 658 AA; 74743 MW; E0EA2713E1232378 CRC64;
MSLRLGVCYY PEHWPEAMWD SDAQRMKALG IKQVRIGEFA WSRIEPSPGE LRWDWLDRAI
EVLARHGLEV VMCTPTATPP KWLIDRHDDV LAVDANGRQR AFGSRRHYDF SSDSYFEESQ
RIVRLLGERY GQHPAVTAWQ TDNEYGCHQT VVSYSASAQR RFRQWLRQRY GSIDALNTAW
GTVFWSMEYR SFDEIDAPIG TVTEAHPSHR LDYRRFASDE VARYNRMQVE ILRALSPGRL
MVHNFMQMFL EFDHYPVAAD LDVATWDSYP LGALEVMWFD DATKARWLRT GHPDFASFNH
DLYRGMSAQP FWVMEQQPGP VNWAHWNPHP LPGMVRLWSW EAFAHGAGCV SYFRWRQCPF
AQEQLHAGLN RPDNRLDVGG SEAEQVAREI ITVEQAQGAL AQPRGKVALL FDYDAKWLFD
IHFQGIDFEY QRFAFQYYAT LRALGLDVDI LPLHAKLDGY AMIVVPPLPI VPDDLPGRIA
ESGALSVFGP RSGSKTRSLQ IPATLPPGPL QQLLPMRVWR VESLRPNVTE PVQFGAHSGQ
GAHWRDLIEA DGEGLQTLAQ FGDGHPAIVR KERAHYLAGI FDDALTSACF EQLARDAGLA
PQRLPEGLRL QERGGLCFAF NYSDAAITLP QAQGAQFLVG QAQLEPQGVA VYRTGQHP
//
