ID A0Z894_9GAMM Unreviewed; 665 AA.
AC A0Z894;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=MGP2080_08349 {ECO:0000313|EMBL:EAW39822.1};
OS marine gamma proteobacterium HTCC2080.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW39822.1, ECO:0000313|Proteomes:UP000004719};
RN [1] {ECO:0000313|EMBL:EAW39822.1, ECO:0000313|Proteomes:UP000004719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW39822.1,
RC ECO:0000313|Proteomes:UP000004719};
RX PubMed=20472793; DOI=10.1128/jb.00511-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT OM60/NOR5 clade of the Gammaproteobacteria.";
RL J. Bacteriol. 192:3842-3843(2010).
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}.
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:EAW39822.1}.
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DR EMBL; AAVV01000013; EAW39822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Z894; -.
DR eggNOG; COG1874; Bacteria.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000004719; Unassembled WGS sequence.
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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; 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; 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};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Reference proteome {ECO:0000313|Proteomes:UP000004719}.
FT DOMAIN 18..406
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 417..609
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 155
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 665 AA; 75578 MW; A7B943D0EE721841 CRC64;
MAEQHFVGGF SELALGVCYY PEHWPEQDWA DDAAQMRALG LRCVRIGEFA WSRLEPQRDQ
FDFGWLDRAI ATLAAENLKV VLCTPTATPP KWLIDEYPEI LPKDPISGRE RGFGSRRHYD
FSSAKYRDEA VRISTILAKR YGDDSRVIGW QTDNELCCHD TAHSWSDSAR QSFQGWCQER
YGTIAHLNTA WGNVFWSMEY PSFSAIELPF GTVTETNPAH QIAYRRFASD QILRFHDACC
SAIRDHASNQ WITHNFIPMK DTQTDCFSLA APLDFVSYDS YPLGRSEFLL GRDEPELARR
YMRTGHPDYT AYYLDQCRGL KDRGFWIMEQ QPGPVNWAPS NPRPAPGMVT LWTLEAIAHG
ADVVSYFRWR QAQFAQEQMH AGLLRPDRSR SDAWQEIETV VAALKTLENA SLPQPRAHVA
LVTDVSAQWV SDIEQQGREV EAHRVTFQFY RALRQLNVTV DIVSPSADLS QYALVVVASM
PIVSDTLLEA CEQSDATLLF GPRCGAKTDE FQIPTNRAPG VLQSWLDLQV NSVETLRPDV
VEPFEYKGKV FQSRLWCEDL AVTNATIEAF YQDKRPALVR KGRCLYLATL TDDAFLRQLL
GDLLTEREIV IQELPEDVRM MTRGSVTFAF NYGKEAHTLD APPSAQVLAG SAKLPPRGFC
IWRSE
//
