ID   A0A1G6H8M3_9MICO        Unreviewed;       438 AA.
AC   A0A1G6H8M3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:SDB90637.1};
GN   ORFNames=SAMN05216410_0837 {ECO:0000313|EMBL:SDB90637.1};
OS   Sanguibacter gelidistatuariae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=1814289 {ECO:0000313|EMBL:SDB90637.1, ECO:0000313|Proteomes:UP000199039};
RN   [1] {ECO:0000313|EMBL:SDB90637.1, ECO:0000313|Proteomes:UP000199039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISLP-3 {ECO:0000313|EMBL:SDB90637.1,
RC   ECO:0000313|Proteomes:UP000199039};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) 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}.
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DR   EMBL; FMYH01000001; SDB90637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6H8M3; -.
DR   STRING; 1814289.SAMN05216410_0837; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000199039; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 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.
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:UP000199039}.
FT   DOMAIN          195..400
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   SITE            109
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   438 AA;  48171 MW;  DADFFE3E6EE36D27 CRC64;
     MVRIAFIGAG SVVFTRQLVA DLLRYDELSD VHLVLHDIDP ARLVAAEGSA RRIDAQLGTS
     ATVTATLDRR TALTGADFVI TMIQVGGIDA TITDLEIPAR HGLRQTIGDT TGVGGVFRAL
     RTFPVLEAIT ADMREVCPDA LLLNYTNPMA MNVWWASVVA PDIQAVGLCH SVYWTAHDLA
     EVVGIPVEET RFRAAGVNHQ AWLLEWTHEG RDLYPTLRER ILADPGLERR ARVEIFRRIG
     YYPTETSEHS AEYLPWFLRS DEQIERFRIE PLQYIDISRE NVADFESTQR LLLTDAPVPL
     EEGASEYAPQ VIHSIVTGTR REIHGNVINR GLVDNLPEGA VVEVPCIVDG DGLVPVPMGA
     LPAQCAALNR PYLSVAELTV EAARTGDPRL LRQAVLMDPN ASSTLTPEQI WILCDELVVA
     HGDLLPEPLR APLPASAL
//