ID C2FDH4_LACPA Unreviewed; 474 AA.
AC C2FDH4;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=6-phospho-beta-galactosidase {ECO:0000256|HAMAP-Rule:MF_01574};
DE EC=3.2.1.85 {ECO:0000256|HAMAP-Rule:MF_01574};
DE AltName: Full=Beta-D-phosphogalactoside galactohydrolase {ECO:0000256|HAMAP-Rule:MF_01574};
DE Short=PGALase {ECO:0000256|HAMAP-Rule:MF_01574};
DE AltName: Full=P-beta-Gal {ECO:0000256|HAMAP-Rule:MF_01574};
DE Short=PBG {ECO:0000256|HAMAP-Rule:MF_01574};
GN Name=lacG {ECO:0000256|HAMAP-Rule:MF_01574,
GN ECO:0000313|EMBL:EEI68030.1};
GN ORFNames=HMPREF0530_1632 {ECO:0000313|EMBL:EEI68030.1};
OS Lacticaseibacillus paracasei subsp. paracasei ATCC 25302 = DSM 5622 = JCM
OS 8130.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=525337 {ECO:0000313|EMBL:EEI68030.1, ECO:0000313|Proteomes:UP000003495};
RN [1] {ECO:0000313|EMBL:EEI68030.1, ECO:0000313|Proteomes:UP000003495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25302 {ECO:0000313|EMBL:EEI68030.1,
RC ECO:0000313|Proteomes:UP000003495};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-phospho-beta-D-galactoside + H2O = an alcohol + D-
CC galactose 6-phosphate; Xref=Rhea:RHEA:24568, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:58534, ChEBI:CHEBI:91004; EC=3.2.1.85;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01574,
CC ECO:0000256|RuleBase:RU004469};
CC -!- PATHWAY: Carbohydrate metabolism; lactose degradation; D-galactose 6-
CC phosphate and beta-D-glucose from lactose 6-phosphate: step 1/1.
CC {ECO:0000256|HAMAP-Rule:MF_01574, ECO:0000256|RuleBase:RU004469}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|HAMAP-Rule:MF_01574}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEI68030.1}.
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DR EMBL; ACGY01000111; EEI68030.1; -; Genomic_DNA.
DR RefSeq; WP_003589794.1; NZ_GG670158.1.
DR AlphaFoldDB; C2FDH4; -.
DR SMR; C2FDH4; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GeneID; 57091558; -.
DR HOGENOM; CLU_001859_1_3_9; -.
DR UniPathway; UPA00542; UER00605.
DR Proteomes; UP000003495; Unassembled WGS sequence.
DR GO; GO:0033920; F:6-phospho-beta-galactosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR HAMAP; MF_01574; LacG; 1.
DR InterPro; IPR005928; 6P-beta-galactosidase.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR01233; lacG; 1.
DR PANTHER; PTHR10353:SF340; 6-PHOSPHO-BETA-GALACTOSIDASE 1; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_01574};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01574}.
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 19
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 116
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 159
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 160
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 297
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 433
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 434
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 440
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
FT BINDING 442
FT /ligand="D-galactose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:91004"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01574"
SQ SEQUENCE 474 AA; 53968 MW; EBE1B0C3A45498C9 CRC64;
MSKQLPQDFV MGGATAAYQV EGATKEDGKG RVLWDDFLDK QGRFKPDPAA DFYHRYDEDL
ALAEKYGHQV IRVSIAWSRI FPDGAGEVEP RGVAFYHKLF ADCAAHHIEP FVTLHHFDTP
ERLHEAGDWL SQEMLDDFVA YAKFCFEEFS EVKYWITINE PTSMAVQQYT SGTFPPAESG
RFDKTFQAEH NQMVAHARIV NLYKSMQLGG QIGIVHALQT VYPYSDSAVD HHAAELQDAL
ENRLYLDGTL AGEYHQETLA LVKEILDANH QPMFQSTPQE MKAIDEAAHQ LDFVGVNNYF
SKWLRAYHGK SETIHNGDGT KGSSVARLQG VGEEKLPDGI ETTDWDWSIY PRGMYDILMR
IHNDYPLVPV TYVTENGIGL KESLPENATP DTVIEDPKRI DYVKKYLSAM ADAIHDGANV
KGYFIWSLQD QFSWTNGYSK RYGLFFVDFP TQNRYIKQSA EWFKSVSETH IIPD
//
