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Database: UniProt/TrEMBL
Entry: V9WMZ2_9RHOB
LinkDB: V9WMZ2_9RHOB
Original site: V9WMZ2_9RHOB 
ID   V9WMZ2_9RHOB            Unreviewed;       639 AA.
AC   V9WMZ2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=Gal_02759 {ECO:0000313|EMBL:AHD10492.1};
OS   Phaeobacter gallaeciensis DSM 26640.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1423144 {ECO:0000313|EMBL:AHD10492.1, ECO:0000313|Proteomes:UP000018782};
RN   [1] {ECO:0000313|EMBL:AHD10492.1, ECO:0000313|Proteomes:UP000018782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26640 {ECO:0000313|EMBL:AHD10492.1,
RC   ECO:0000313|Proteomes:UP000018782};
RA   Frank O., Petersen J., Goeker M., Klenk H.-P., Rohde M., Scheuner C.;
RT   "Complete genome sequence of the Phaeobacter gallaeciensis type strain CIP
RT   105210T.";
RL   Submitted (DEC-2013) 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; CP006966; AHD10492.1; -; Genomic_DNA.
DR   RefSeq; WP_024098123.1; NZ_AOQA01000007.1.
DR   AlphaFoldDB; V9WMZ2; -.
DR   GeneID; 31847127; -.
DR   KEGG; pgd:Gal_02759; -.
DR   PATRIC; fig|1423144.3.peg.2763; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_5; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000018782; 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: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, ECO:0000313|EMBL:AHD10492.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:AHD10492.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018782};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          8..393
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          402..591
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        144
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        316
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         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   639 AA;  71503 MW;  5A83C2A722C20CA7 CRC64;
     MQRTLGTCYY PEHWPEDIWQ EDAARMVAAG LTWVRIGEFS WSRIEPTPGD LQWDWLDRAI
     NTLGAAGLKV VLGTPTATPP RWMVDRHPDM FALDADGKPR GFGSRRHYCF SHKGYRAEAR
     RIVTLMAERY GPGGRIAAWQ TDNEYGCHDT TISYSDSARV AFVRWLEERY NGDICALNAA
     WGNVFWSMEY ERFDQIGLPN LTVTEPNPAH VQAFRRFSSD QVVSFNRDQV EILRAHSDAP
     IAHNYMGRVT DFDHYKVGVD LEIASWDSYP LGFLEDRVGA SPEDQRRYAR QGDPDFQAFH
     HDLYRAVGRG RWWVMEQQPG PVNWAPYNPA PLPGMVRFWT WEAFAHGAEA VCYFRWRQAP
     FAQEQLHAGL LRPDSAETPA ISEARQVAEE LASAGEVGPS QAPVALIFDY DAEWAWQVQP
     HGQGLSYFDL VLDHYRALRR AGLSVDIVPP TQSDFTGYEL ILAPGLMHLP DDLRRALADA
     PGLRLYGPRT AARDEDFKIP TAPLPPALQG LDVVIAAVES LRPDMPLPLA NGDGAVVCYL
     ETLEGEADVL FETSTGHAVA VAAGNQVYCA GWLDMAGLDC LIATLCARAG VTIRKMPQGV
     RVRQTATEEF WFNHLAEPVE AVVGTLPPAG VLRRARQEV
//
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