ID A0A061ABM4_9MOLU Unreviewed; 431 AA.
AC A0A061ABM4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glycoside hydrolase, family 4 {ECO:0000313|EMBL:CDR31270.1};
GN ORFNames=Aocu_11970 {ECO:0000313|EMBL:CDR31270.1};
OS Acholeplasma oculi.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Acholeplasma.
OX NCBI_TaxID=35623 {ECO:0000313|EMBL:CDR31270.1, ECO:0000313|Proteomes:UP000032434};
RN [1] {ECO:0000313|Proteomes:UP000032434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kube M.;
RL Submitted (MAY-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR EMBL; LK028559; CDR31270.1; -; Genomic_DNA.
DR RefSeq; WP_045749704.1; NZ_UFRU01000001.1.
DR AlphaFoldDB; A0A061ABM4; -.
DR STRING; 35623.Aocu_11970; -.
DR KEGG; aoc:Aocu_11970; -.
DR PATRIC; fig|35623.3.peg.1197; -.
DR HOGENOM; CLU_045951_0_1_14; -.
DR InParanoid; A0A061ABM4; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000032434; 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 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Reference proteome {ECO:0000313|Proteomes:UP000032434}.
FT DOMAIN 197..402
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 431 AA; 49327 MW; 12F0E0C9A30C4A2A CRC64;
MSVKTKITVI GAGSSYTPEV IGKIIDYQHT LKVDEISLLD LEDNLDRLKI IHQYSQRMIE
ANNETIRISY TLDRKEALED ATFVLIQIRV GKMEARIFDE TIPSLYGLLG HETIGIGGMF
NALRTVPVIY EIIEDVKKYA PKAWVINVSN PSGIIAEAVY RFSEFDRFIG ISSDPNQATK
TLQQKLNASP GEVVPYFAGL NDLSFILKVY HHGKDKLDSL IEEGYSPYKE GMESLIFKDM
RLFSHPNLRY YYHHDEMLKA YLDDMKKGSI RAKEVVSIEQ QLFEKFKDEK TIDLPKNMDQ
RLGRNYADTA IGIMDAIKNN TKAYHVINTV NRGHILGIPD ECAIEITSRM TNRGPIPVHI
GELPLQVRGI IQHLKAYEEL LCDAIYERDL DKALLAIQTH PLSRSFNQNK VTFKKLVEAH
EKHLTYYRKD S
//
