ID A0A084JQP7_9FIRM Unreviewed; 442 AA.
AC A0A084JQP7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Diacetylchitobiose-6-phosphate hydrolase {ECO:0000313|EMBL:KEZ91281.1};
GN ORFNames=IO98_04355 {ECO:0000313|EMBL:KEZ91281.1};
OS Lacrimispora celerecrescens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=29354 {ECO:0000313|EMBL:KEZ91281.1, ECO:0000313|Proteomes:UP000028525};
RN [1] {ECO:0000313|EMBL:KEZ91281.1, ECO:0000313|Proteomes:UP000028525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=152B {ECO:0000313|EMBL:KEZ91281.1,
RC ECO:0000313|Proteomes:UP000028525};
RA Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT "Draft genome of Clostridium celerecrescens 152B isolated from sediments
RT associated with methane hydrate from Krishna Godavari basin.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KEZ91281.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPME01000006; KEZ91281.1; -; Genomic_DNA.
DR RefSeq; WP_038278241.1; NZ_JPME01000006.1.
DR AlphaFoldDB; A0A084JQP7; -.
DR STRING; 29354.IO98_04355; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000028525; 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; cd05296; GH4_P_beta_glucosidase; 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:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 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:UP000028525}.
FT DOMAIN 197..413
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 149
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 SITE 111
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 442 AA; 49703 MW; A1489216B22F292F CRC64;
MEGIKIVTIG GGSSYTPELV EGFIKRYEKL PVRELWLVDI EEGREKLETV GALAQRMVKK
AGLPMKVILS YDRREALKDA DYVTTQMRVG LLEARIKDER IPLSHGMIGQ ETNGAAGMFK
AFRTIPVILD IVKDMKELCP EAWMINFTNP AGMITEAVLR YTDYKKVIGL CNVPINMVNG
FARLLDVEPE RVTMELSGLN HHIFATDVFV DGQSRLEEIL EIYQHISAED AISMKNFSTL
PFSPEFIRGL HCIPCPYHNY YFFTKEQLEE ELKEYKEGRV RGEVVKKVEE ELFELYKDEN
LDVKPKQLEM RGGARYSDAA CNLICSLHNN TGDIQYVDVR NNGTISNLPA DSAVEVACII
TSGGPKPIAV GELKPQINGT IQTIKTFERL VCEAAVTGNR DLAVTALNMN PLCASDHDAN
AVIDELLEAH KKHLPQFFNF IK
//