ID A0A0H3E4J4_BACA1 Unreviewed; 444 AA.
AC A0A0H3E4J4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycosyl hydrolase family 4 C-terminal domain-containing protein {ECO:0000259|Pfam:PF11975};
GN OrderedLocusNames=BATR1942_11660 {ECO:0000313|EMBL:ADP33263.1};
OS Bacillus atrophaeus (strain 1942).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP33263.1, ECO:0000313|Proteomes:UP000006867};
RN [1] {ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA Rosenzweig C.N., Skowronski E.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP33263.1, ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|EMBL:ADP33263.1,
RC ECO:0000313|Proteomes:UP000006867};
RX PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA Skowronski E.W.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus var. globigii, a historical biowarfare simulant.";
RL PLoS ONE 6:E17836-E17836(2011).
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; CP002207; ADP33263.1; -; Genomic_DNA.
DR RefSeq; WP_003325267.1; NC_014639.1.
DR AlphaFoldDB; A0A0H3E4J4; -.
DR GeneID; 23410773; -.
DR KEGG; bae:BATR1942_11660; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_0_1_9; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000006867; 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; 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}.
FT DOMAIN 195..410
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 110
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 444 AA; 49944 MW; B83EEE66DC96A126 CRC64;
MALKLVIIGG GSSYTPEIIE GIIKRYQHFP VKEVVLVDIE EGEEKVRITS ELAKRMIKHA
DVPIELSYTK DRARALKHAD FVTVQIRVGG LNARSLDERI PLSHGLIGQE TNGAGGIFKA
LRTIPVMLDI ARDIKEICPE AWLINFTNPA GIVTEALLKH GPHQKVIGVC NIPYNMKNSI
AEIFDVNVNR VMIEFAGLNH FVFGQKVWID GVDRTEEAIG HLLNDTIDYS PSNIAMLPWN
RQFLRSLRML PNPYHQYYYQ YEDVLAKDIE AYKNKGTRAE AVMDVEKQLF EKYNDADIHE
KPKELEERGG AYYSEAACSL MNSLYHHSMD IQTVNTLNRG SIPDLPHDAV IEVNSVITKS
GPIPLTVGKL PDSISGAVIS IKKFEQLVIE AAITGDDNIL YSAMIMNPLI PSDHKAQSVM
NEMLEAHKRY LPQFFKEAVH DETK
//
