ID C5BFJ3_EDWI9 Unreviewed; 450 AA.
AC C5BFJ3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Alpha-galactosidase, putative {ECO:0000313|EMBL:ACR68956.1};
DE EC=3.2.1.22 {ECO:0000313|EMBL:ACR68956.1};
GN OrderedLocusNames=NT01EI_1777 {ECO:0000313|EMBL:ACR68956.1};
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR68956.1, ECO:0000313|Proteomes:UP000001485};
RN [1] {ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR68956.1, ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|EMBL:ACR68956.1,
RC ECO:0000313|Proteomes:UP000001485};
RX PubMed=22247535; DOI=10.1128/JB.06522-11;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA Lawrence M.L.;
RT "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL J. Bacteriol. 194:740-741(2012).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR EMBL; CP001600; ACR68956.1; -; Genomic_DNA.
DR RefSeq; WP_015871104.1; NC_012779.2.
DR AlphaFoldDB; C5BFJ3; -.
DR STRING; 67780.B6E78_02015; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR GeneID; 69538745; -.
DR KEGG; eic:NT01EI_1777; -.
DR PATRIC; fig|634503.3.peg.1593; -.
DR HOGENOM; CLU_045951_1_1_6; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000001485; 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; 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 197..420
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 450 AA; 50190 MW; 2C9C3C854A01AF46 CRC64;
MNAPKIAFIG AGSTIFVKNI LGDVFQRPAL RGADIALMDI DAQRLAESRI VVGRLMAAAG
ADGHIQCHTT LRPALQGADF VVVAFQIGGY TPCTVTDFEV CARHGLRQTI GDTLGPAGIM
RALRTFPHLW QIGEMMMAEC PQATLLNYVN PMAMNSWAMY ARYPQLRQVG LCHSVQGTAE
ELARDLDIDP AQLRYRCAGI NHMAFYLSLE QRGGDGQYRD LYPQLLQAYR QGRAPKPNIH
GNLRCENIVR YELLQKLGYF VTESSEHMAE YTPWFIKPGR DDLIARYRIP LDEYPKRCVE
QMASWQRELA EYQAAPHIEI TPSREYASRI MNALWSGEPE VIYGNVRNAG LIDNLPQGCC
VEVPCLVDAN GIQPTRIGSL PSHLAALMQT NVNVQTLVTE AALTENRERI YHAALLDPHT
AATLSIDEIY ALIDDLIAAH GDWLPDWVRG
//
