ID B9MRA1_CALBD Unreviewed; 438 AA.
AC B9MRA1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Glycoside hydrolase family 4 {ECO:0000313|EMBL:ACM60205.1};
GN OrderedLocusNames=Athe_1104 {ECO:0000313|EMBL:ACM60205.1};
OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / KCTC 15123 /
OS Z-1320) (Anaerocellum thermophilum).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=521460 {ECO:0000313|EMBL:ACM60205.1, ECO:0000313|Proteomes:UP000007723};
RN [1] {ECO:0000313|Proteomes:UP000007723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320
RC {ECO:0000313|Proteomes:UP000007723};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kataeva I., Adams M.W.W.;
RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}.
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DR EMBL; CP001393; ACM60205.1; -; Genomic_DNA.
DR RefSeq; WP_015907610.1; NC_012034.1.
DR AlphaFoldDB; B9MRA1; -.
DR STRING; 521460.Athe_1104; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR GeneID; 31772455; -.
DR KEGG; ate:Athe_1104; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_1_1_9; -.
DR Proteomes; UP000007723; 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; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR Gene3D; 3.90.1820.10; AglA-like glucosidase; 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; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 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 193..408
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 109
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 438 AA; 49748 MW; A544B81DB4658C3B CRC64;
MLKIAIIGAG SGVFTRNLVR DILSYPELRN STIALMDIDS IRLEFMRKAL QKLIEQEKYP
TKLEATTDRK EALKGAKYVI VTIQIGGLKP FEYDIYIPLK YGVKQAVGDT IGPGGVFRAL
RTILVLLDIA KDMEELCPDA LLLNYVNPMA MNCWALNKAT NIKNVGLCHS VQGTAEFLAK
IIGAKMEEIS YLCAGINHMA WFLKFEWNGK DAYPLIREKA SDPEIYTQDV TKFEILKHFG
YYVTESSFHM SEYVPYFRKS DDWINKIHRT HSWHKEHYNG MYLHCCLDAA KTLLEDLRKM
AEADYIDPKR SNEYCATIIH SIETNTPAVI NGNVENKGLI TNLPEGCCVE VPCLVDKNGI
QPTYVGNLPP QLAALNRTNI NVQELTVLAA LTGDREAVYH AIMMDPLTSA VLDLDQIRQM
VDEMFEAEKE WLPEKFYR
//
