ID Q6ABV2_CUTAK Unreviewed; 462 AA.
AC Q6ABV2;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=Glucosidase {ECO:0000313|EMBL:AAT81821.1};
GN OrderedLocusNames=PPA0061 {ECO:0000313|EMBL:AAT81821.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT81821.1, ECO:0000313|Proteomes:UP000000603};
RN [1] {ECO:0000313|EMBL:AAT81821.1, ECO:0000313|Proteomes:UP000000603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT81821.1; -; Genomic_DNA.
DR RefSeq; WP_002515923.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6ABV2; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR EnsemblBacteria; AAT81821; AAT81821; PPA0061.
DR KEGG; pac:PPA0061; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_0_1_11; -.
DR Proteomes; UP000000603; Chromosome.
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; 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.
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 203..434
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 106
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 462 AA; 49964 MW; 514A866C1EFD08FA CRC64;
MKLTILGGGG FRVPLVFKAL AHDTSPQRVT ELRLYDTDPL RLGVIETVVA QLARALPHAP
SVVATTDLPT ALAGTDFIFS AIRVAGTHGR ALDESMCLAR GVIGQETVGA GGISYALRGI
PVVLDLVEQI TRYAPDAKVI NFTNPAGVMT EVMQRRLGDQ VVGICDSPVG LARRILTTLQ
RAGLAPADLG SLFDGDGRIH IGYSGLNHLG WLTSLNVDGV DVLPRLLERP DLIESFEEGR
LFGADLVQAL GAVPNEYLHY YYYSRDDLAA DRKAEAPRGA FLEAQQNQFY TQAQHTDDVA
GLWEATRLER EETYMATNRE VSGEFERDEA DLETGGYDKV ALAIMHAIAN DVPAELILNV
ANHGALPDLP DEAVVEVPCR VDGAGIHRLP TPALPDHARG LVVNAKYVEQ RTIDAAVNHS
RTAALLALSH HPLVDSVHVA EQLLDDFADA FDGLEYLKDA HA
//
