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Database: UniProt
Entry: L8TUC3_9MICC
LinkDB: L8TUC3_9MICC
Original site: L8TUC3_9MICC 
ID   L8TUC3_9MICC            Unreviewed;       467 AA.
AC   L8TUC3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Family 4 glycosyl hydrolase, alpha-galactosidase/6-phospho-beta-glucosidase {ECO:0000313|EMBL:ELT45385.1};
GN   ORFNames=G205_05941 {ECO:0000313|EMBL:ELT45385.1};
OS   Arthrobacter nitrophenolicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT45385.1, ECO:0000313|Proteomes:UP000011189};
RN   [1] {ECO:0000313|Proteomes:UP000011189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX   PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA   Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT   "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT   Arthrobacter sp. Strain SJCon.";
RL   Genome Announc. 1:e0005813-e0005813(2013).
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}.
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:ELT45385.1}.
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DR   EMBL; AOFD01000009; ELT45385.1; -; Genomic_DNA.
DR   RefSeq; WP_009357031.1; NZ_AOFD01000009.1.
DR   AlphaFoldDB; L8TUC3; -.
DR   PATRIC; fig|683150.5.peg.1189; -.
DR   Proteomes; UP000011189; 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; 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:UP000011189}.
FT   DOMAIN          192..438
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        165
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        246
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            105
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   467 AA;  49365 MW;  71E31E459A952AAA CRC64;
     MRLLIAGGGG FRVPLVYRAL ASGRFAGLVS ELVLYDVDPS RLAAVTAVLR SMPGPGAGPP
     VRATTSLPDA LAGTQMVFAA VRPGGTAGRV ADEKVAQDLG LLGQETTGAG GISYALRTIP
     HMLGLARQMR EHSPEAWLIN FTNPAGMVTE ALVPVLGSRV IGICDSAGGL VQRAARAAGV
     ALPDGRLDGV GYYGLNHLGW LYRLESGGRD VLPGLLADPR ALQSFEEGRL FPQPFLAGLG
     ALPNEYLYYY YRLDDARRAM RAMPVTRGES IHLQQQELYP RLAAAGTDAY RLWEEARRSR
     EEGYLAEARA NGEQRDEDDL AGGGYERVAL AAMRALSGAG DTQLILNTRN SLPAASNAAT
     AEAPPARAAI PGPPADAVVE LPCTVTPDGA LPLPQAEPGK EQMELLRRVK EVERLTVLAA
     TEGTRDAALA AFARHPLVDS PDLASDLLAG YEHAFPALRK LWGGGAA
//
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