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Database: UniProt
Entry: A0A0D0QBV3_9RHOB
LinkDB: A0A0D0QBV3_9RHOB
Original site: A0A0D0QBV3_9RHOB 
ID   A0A0D0QBV3_9RHOB        Unreviewed;       453 AA.
AC   A0A0D0QBV3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:KIQ69757.1};
DE            EC=3.2.1.22 {ECO:0000313|EMBL:KIQ69757.1};
GN   ORFNames=Wenmar_01327 {ECO:0000313|EMBL:KIQ69757.1};
OS   Wenxinia marina DSM 24838.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Wenxinia.
OX   NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ69757.1, ECO:0000313|Proteomes:UP000035100};
RN   [1] {ECO:0000313|EMBL:KIQ69757.1, ECO:0000313|Proteomes:UP000035100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ69757.1,
RC   ECO:0000313|Proteomes:UP000035100};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU361152};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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:KIQ69757.1}.
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DR   EMBL; AONG01000008; KIQ69757.1; -; Genomic_DNA.
DR   RefSeq; WP_018301312.1; NZ_KN848372.1.
DR   AlphaFoldDB; A0A0D0QBV3; -.
DR   STRING; 1123501.Wenmar_01327; -.
DR   PATRIC; fig|1123501.6.peg.1411; -.
DR   eggNOG; COG1486; Bacteria.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000035100; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR   Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW   Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035100}.
FT   DOMAIN          195..417
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            110
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   453 AA;  50783 MW;  CD0A1EE04703BA70 CRC64;
     MTIVTFIGAG STVFARNLAG DILQRPALRD ATIRLMDIDR KRLEESEIVV GKMARTLGGH
     ATVETYTDRR RALDGADFVI CCLQVGGYEP CTVTDFEIPK KFGLRQTIAD TLGIGGIMRG
     LRTVPVLWDI CADMREVCPD ALMLQYVNPM AINTWGIGAK FPDIRQVGLC HSVQGTAEEL
     ARDLEIPIGE IRYHCAGINH MAFYLRFEHR QPDGSYRDLY PALRQGYREG RFPKPSSWNP
     RCPNKVRYEM LMRLGHFVTE SSEHFAEYVP YFIKRDRPDL IERFGIPLDE YPKRCVEQIA
     RWESEAQAYR EADEVVVKPS HEYASEIVNS VVTGAPSVVY GNIPNRGYIP QLPQGAAVEV
     PVLVDANGLQ PTMVEGIPPQ LIALMRTNVN VQELTVAALV EEKVEHLYHA AMLDPHTAAE
     LDLDQIWELT GELLAAHGEW VPEWARVGVK GAA
//
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