ID A0A0J0Y2J5_9SPHI Unreviewed; 450 AA.
AC A0A0J0Y2J5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glycosyl hydrolase family 109 {ECO:0000313|EMBL:KLT64466.1};
GN ORFNames=AB669_16485 {ECO:0000313|EMBL:KLT64466.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT64466.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT64466.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT64466.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000256|ARBA:ARBA00009329}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLT64466.1}.
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DR EMBL; LECU01000007; KLT64466.1; -; Genomic_DNA.
DR RefSeq; WP_047800749.1; NZ_LECU01000007.1.
DR AlphaFoldDB; A0A0J0Y2J5; -.
DR STRING; 1663685.AB669_16485; -.
DR PATRIC; fig|1663685.3.peg.3452; -.
DR OrthoDB; 9771072at2; -.
DR Proteomes; UP000036014; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR049303; Glyco_hydro_109_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF1; GLYCOSYL HYDROLASE FAMILY 109 PROTEIN; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF21252; Glyco_hydro_109_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KLT64466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036014}.
FT DOMAIN 34..160
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 172..353
FT /note="Glycosyl hydrolase 109 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21252"
SQ SEQUENCE 450 AA; 50373 MW; 03BDAE1AABDFD6DB CRC64;
MNRREFVRNA GLTTAAIATI PDQTLFAAQA DGKIKVVMIG VGLRGQNHLS LILRRDDVEL
VAICDVDDKM LQMSKAIVSK SGKPMPRIFT GDENAWKKML ELKNIKAVII ATPWELHKPM
ILGALDAGIK YIATEVILGI NLQDHWDVVH ATEKADAHVM MLENVCYRRD VLAALNMVRQ
GLFGEMLHLQ GGYQHDLREV KFNDGVNPYG HGVEFGEKAF SEARWRTNHS VYRNGDLYPT
HGIGPVAQCI NINRGNRFLK LNSFATKSRG LHNYIVDKGG AAHPNAKVNF RLGDIVTTTI
DCANGETIIL QHDTNLPRPY SLGFRFQGTK GLWMDINKSI YVEGVSKPHT WDNAKEWLDK
YDHPLWKKYG NDAQGAGHGG MDFFVIHAFI EAAKRNEATP LDIYDAAAWS AITPLSEQSI
ELGNETVEFP DFTGGKWMSR KPIFALNDDY
//