ID I6B184_9BACT Unreviewed; 734 AA.
AC I6B184;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Family 4 glycosyl hydrolase, alpha-galactosidase/6-phospho-beta-glucosidase {ECO:0000313|EMBL:EIQ01026.1};
GN ORFNames=OpiT1DRAFT_05588 {ECO:0000313|EMBL:EIQ01026.1};
OS Opitutaceae bacterium TAV1.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278956 {ECO:0000313|EMBL:EIQ01026.1, ECO:0000313|Proteomes:UP000004921};
RN [1] {ECO:0000313|EMBL:EIQ01026.1, ECO:0000313|Proteomes:UP000004921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV1 {ECO:0000313|EMBL:EIQ01026.1,
RC ECO:0000313|Proteomes:UP000004921};
RX PubMed=22535930; DOI=10.1128/JB.00264-12;
RA Isanapong J., Goodwin L., Bruce D., Chen A., Detter C., Han J., Han C.S.,
RA Held B., Huntemann M., Ivanova N., Land M.L., Mavromatis K., Nolan M.,
RA Pati A., Pennacchio L., Pitluck S., Szeto E., Tapia R., Woyke T.,
RA Rodrigues J.L.;
RT "High-Quality Draft Genome Sequence of the Opitutaceae Bacterium Strain
RT TAV1, a Symbiont of the Wood-Feeding Termite Reticulitermes flavipes.";
RL J. Bacteriol. 194:2744-2745(2012).
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; JH660698; EIQ01026.1; -; Genomic_DNA.
DR AlphaFoldDB; I6B184; -.
DR HOGENOM; CLU_377587_0_0_0; -.
DR Proteomes; UP000004921; 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}.
FT DOMAIN 195..403
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 149
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 734 AA; 79468 MW; 6C13ECECA6E324CD CRC64;
MPKITLIGAG SVVFAKNLIS DILQFPELSD ATLALMDIDP ARLETARVMT ERVIRKLGVK
ARVEVFSDRR KAVAGANYVI CTIQVGGYKP GTVIDFEIPR KYGLLQTIGD TLGVGGVFRG
LRTIPRILEI ARDIADVGAP GCTFLNYTNP MAMLCMAVDH AVGVPTVGLC HSVQGTSQQL
AGYAGLDFDH VTYRVAGINH MAFFLDYKYR GQDAYPFLFK LLDDPAFTQD KVRFEMMRRL
GYFVTESSEH QSEYNPHFIH HGKEVIKKFD IPIDEYLRRC ESIIATWKKA EAELIGADGD
IVVNPQTHEY GSFIIHSMET NTPRVIYGNV PNRNLITNLP HRCCVELPVL VDAQGLQPTY
IGDLPPQLAA ICRTNINVQE LTVAAALTGK REHIYHAVMT DPHAAATLPL DKIWAMCDDL
IEAHQKAGLL GEYAPVISNT GRTRAGTGDK VLVSLEPVKT LTALDAATPV EFVLTATNQG
DKPFSGPLAI EAGPVAVTLG GSGSAAGGNT LALPVGPGKT VSKRIKLRPA ASVAKGPFTV
RVTSSDPRVL GHDYVFKERR LVSGAAAKTG APVEVRFMDN KLLSAQLKLD GTVLELAGRV
LDTAVKIDEG SPWTASAIEL FVNSEHGSRL RQFFLLPREK GITVLNRERQ PFGKKTATAA
FKVKIDKGGY DFTLRLDLAA PGVEVLETGK PGAFFLDLIV AAGALGDAHS SCRVGWNGKL
NSSATSAHYA FVIP
//
