ID C4LB46_TOLAT Unreviewed; 442 AA.
AC C4LB46;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Maltose-6'-phosphate glucosidase {ECO:0000313|EMBL:ACQ94249.1};
DE EC=3.2.1.122 {ECO:0000313|EMBL:ACQ94249.1};
GN OrderedLocusNames=Tola_2655 {ECO:0000313|EMBL:ACQ94249.1};
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ94249.1, ECO:0000313|Proteomes:UP000009073};
RN [1] {ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACQ94249.1, ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RX PubMed=22180815; DOI=10.4056/sigs.2184986;
RA Chertkov O., Copeland A., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA Brettin T., Larimer F., Land M., Hauser L., Spring S., Rohde M.,
RA Kyrpides N.C., Ivanova N., Goker M., Beller H.R., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Tolumonas auensis type strain (TA 4).";
RL Stand. Genomic Sci. 5:112-120(2011).
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; CP001616; ACQ94249.1; -; Genomic_DNA.
DR RefSeq; WP_015879698.1; NC_012691.1.
DR AlphaFoldDB; C4LB46; -.
DR STRING; 595494.Tola_2655; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR KEGG; tau:Tola_2655; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_2_0_6; -.
DR OMA; KYPMREK; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000009073; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050081; F:maltose-6'-phosphate glucosidase 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; cd05298; GH4_GlvA_pagL_like; 1.
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; 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: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.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000009073};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 195..417
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
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 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 285
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 442 AA; 49485 MW; 86A62D2752BA39AD CRC64;
MKKYSVLVAG GGSTFTPGIV LMLLDNLDKF PIKELKFYDN DAARQETIGK ACAVLIKERA
PEVVFSYTTD PREAFSGVDF VMAHIRVGKY PMRELDEKIP LKYGVVGQET CGPGGIAYGM
RSIGGVLELV DYMEKYSPNA WMLNYSNPAA IVAEATRSMR PNSKILNICD MPVGIEVRMA
EILGLESRKE MTVKYYGLNH FGWYSDIRDQ AGNDLMPKLK EHVAKYGYVV HKDIDSQHVE
PSWNDTFAKA KDVFALDTNT LPNTYLKYYL FPDYVVEHSD KEYTRANEVM DGREKHVFGE
CRKIAEKGSS AGASLHIDEH ASYIVDLARA IAYNTKERML LIVPNQGSVS NFDPTAMVEI
PCLVGNTGPE PMQIGKIPQF QLGLMNQQVA VEKLVVEAWM EKSYTKLWQA ITLSKTVPSA
SVAKAILDDL IAANKDYWPE LN
//