GenomeNet

Database: UniProt
Entry: A0A084JQP7_9FIRM
LinkDB: A0A084JQP7_9FIRM
Original site: A0A084JQP7_9FIRM 
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
//
DBGET integrated database retrieval system