ID B8D1C3_HALOH Unreviewed; 432 AA.
AC B8D1C3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Glycoside hydrolase family 4 {ECO:0000313|EMBL:ACL71075.1};
DE EC=3.2.1.22 {ECO:0000313|EMBL:ACL71075.1};
GN OrderedLocusNames=Hore_23300 {ECO:0000313|EMBL:ACL71075.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL71075.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL71075.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL71075.1; -; Genomic_DNA.
DR RefSeq; WP_015924043.1; NC_011899.1.
DR AlphaFoldDB; B8D1C3; -.
DR STRING; 373903.Hore_23300; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR KEGG; hor:Hore_23300; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_1_1_9; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000000719; Chromosome.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
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 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.
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:UP000000719}.
FT DOMAIN 195..404
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 149
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 111
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 432 AA; 49312 MW; 573DD08673E99F36 CRC64;
MPKITFLGAG STVFAKNVLG DCMLTPALRD SHIALYDIDH QRLRESEQML KSINRNSNQN
RAEIVAYTDR KEALRDSDYV VNAIQVGGYK PCTVTDFEVP KKYGLRQTIG DTLGIGGIFR
ALRTIPILLD FARDIEEVCP DAWFLNYTNP MAILTGAMLK ATNVKTVGLC HSVQTCVPDL
LKDLGMSTEN VQWKIAGINH MAWLLEITRN GRDLYPEIKE KARARKKPHD DMVRYEIMER
FGYYVTESSE HNAEYMPYFI KSNYPELIEK YNIPLDEYPR RCEQQIKDWE EMKDKLVHND
NLEHSRTHEY ASYIMEAMET DKPYKIGGNV LNTGLITNLP EDACVEVPCL VDRSGVTPCY
VGDLPPQLAA LNRTNINVQL LTIEAALTRK KEYIYQAAML DPHTAAELSI DEIYALVDDM
IEAHGDWLPE YK
//
