ID A7HMR6_FERNB Unreviewed; 472 AA.
AC A7HMR6;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Glycoside hydrolase family 4 {ECO:0000313|EMBL:ABS61199.1};
GN OrderedLocusNames=Fnod_1352 {ECO:0000313|EMBL:ABS61199.1};
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS61199.1, ECO:0000313|Proteomes:UP000002415};
RN [1] {ECO:0000313|EMBL:ABS61199.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS61199.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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; CP000771; ABS61199.1; -; Genomic_DNA.
DR RefSeq; WP_011994507.1; NC_009718.1.
DR AlphaFoldDB; A7HMR6; -.
DR STRING; 381764.Fnod_1352; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR KEGG; fno:Fnod_1352; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_1_1_0; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000002415; 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; 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 NCBIfam; NF041089; alpha_gluc_AglA; 1.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF4; ALPHA-GLUCOSIDASE; 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:UP000002415}.
FT DOMAIN 197..442
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
SQ SEQUENCE 472 AA; 54279 MW; 130F301D6F91B558 CRC64;
MENLKIAIIG AGSAVFSMKI VSDLCKVQKL KGSHVVLMDI DERRLHNVYV LTKELSRVFD
ANLDIETTTD MQKAIEGADF VINTAMAGGH DYLDKVRAIG EKHGYYRGID AQNYNFVSDY
LNLTNWNQFS LFLKIAKMIE KFAPNAWYLQ AANPVFEGTT LVSTQTSIKM VGFCHGHYAV
ESLANLIGVK EYDWQVGGVN HGIWLTKFTT KDGKDLYPEI DKYKGKIQHK PSNPFDDQLS
PVAWDMYDFY GLFPIGDTVR NSTWKYHRDL ETKKRWYGEP WGGADSELGW KWYVEQLYKV
VEIINQFATA IENGLTLEKV KDSMNLMPWL EDDWKNMVNE LLDSEKLSGE QHVPFIDSVV
NGTKRRFVVN MINKGKIKGI DDDVAVEICA WVSGENIEFE ETHLPERVIN WYIKPRVLLA
KQALEAFLKK DTKLVADIIE RDWRTKSSEQ VKKLIDELYP FVIAEMKKII EN
//
