ID A0A1I5A319_9CLOT Unreviewed; 445 AA.
AC A0A1I5A319;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Maltose-6'-phosphate glucosidase {ECO:0000313|EMBL:SFN56786.1};
GN ORFNames=SAMN04488695_102292 {ECO:0000313|EMBL:SFN56786.1};
OS Proteiniclasticum ruminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Proteiniclasticum.
OX NCBI_TaxID=398199 {ECO:0000313|EMBL:SFN56786.1, ECO:0000313|Proteomes:UP000181899};
RN [1] {ECO:0000313|EMBL:SFN56786.1, ECO:0000313|Proteomes:UP000181899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML2 {ECO:0000313|EMBL:SFN56786.1,
RC ECO:0000313|Proteomes:UP000181899};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR EMBL; FOVK01000002; SFN56786.1; -; Genomic_DNA.
DR RefSeq; WP_074911363.1; NZ_FOVK01000002.1.
DR AlphaFoldDB; A0A1I5A319; -.
DR STRING; 398199.SAMN05421804_10220; -.
DR eggNOG; COG1486; Bacteria.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000181899; 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 Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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:SF14; MALTOSE-6'-PHOSPHATE GLUCOSIDASE; 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:UP000181899}.
FT DOMAIN 196..415
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 110
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 445 AA; 50867 MW; 7C1B293651630B9D CRC64;
MRKNPVITIA GAGSLRIPAL IGSLIYYKET LPVAKIILFD IDEERLQRVR AYIDLTLKEY
YSEAEVLFTT KEEEAYGDTD YVLCNMRVGV DTMRSVDEKI PLKYGLVGQE TCGPGGFSYG
MRSIGAMIDM VNTVRTYSKD TWILNYTNPA AIVAVALDKV FPEDKRIMNI CDQPYSMIKS
FAKILGEDMY DLEPRYFGLN HFGWFTSLKN AKTGEELLPK LKDYLMGHEF KPFNAEQRDP
SWLKTYKNVN KLMQFFPEYV PNTYLQYYFF AEEIVQDSDP SFTRVDEAKL GREKKVLDIL
KKAETQGNLT DIPLMQGEVF GNLMVEVVDS IHNDLNKVFV VIGRNGDLIP NLPEDAMVEL
ASYLGKEGAK MIPYGEVKPF YKGLIEGQYA YEKLTVESYL EKDYTKALQA LTLNRSIVDP
VKAKLVLDDL MDHSADYWAL EKKEL
//
