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Database: UniProt
Entry: F0SE07_PSESL
LinkDB: F0SE07_PSESL
Original site: F0SE07_PSESL 
ID   F0SE07_PSESL            Unreviewed;       448 AA.
AC   F0SE07;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Oxidoreductase domain protein {ECO:0000313|EMBL:ADY52933.1};
GN   OrderedLocusNames=Pedsa_2385 {ECO:0000313|EMBL:ADY52933.1};
OS   Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / CCUG
OS   39354 / LMG 10337 / NBRC 100064 / NCIMB 13643) (Pedobacter saltans).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pseudopedobacter.
OX   NCBI_TaxID=762903 {ECO:0000313|EMBL:ADY52933.1, ECO:0000313|Proteomes:UP000000310};
RN   [1] {ECO:0000313|EMBL:ADY52933.1, ECO:0000313|Proteomes:UP000000310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 /
RC   NCIMB 13643 {ECO:0000313|Proteomes:UP000000310};
RX   PubMed=22180808; DOI=10.4056/sigs.2154937;
RA   Liolios K., Sikorski J., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Huntemann M., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA   Kotsyurbenko O., Rohde M., Tindall B.J., Abt B., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of the gliding, heparinolytic Pedobacter saltans
RT   type strain (113).";
RL   Stand. Genomic Sci. 5:30-40(2011).
RN   [2] {ECO:0000313|Proteomes:UP000000310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 /
RC   NCIMB 13643 {ECO:0000313|Proteomes:UP000000310};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Pedobacter saltans DSM 12145.";
RL   Submitted (FEB-2011) 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}.
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DR   EMBL; CP002545; ADY52933.1; -; Genomic_DNA.
DR   RefSeq; WP_013633419.1; NC_015177.1.
DR   AlphaFoldDB; F0SE07; -.
DR   STRING; 762903.Pedsa_2385; -.
DR   KEGG; psn:Pedsa_2385; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OrthoDB; 9771072at2; -.
DR   Proteomes; UP000000310; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000310}.
FT   DOMAIN          33..154
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          169..350
FT                   /note="Glycosyl hydrolase 109 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21252"
SQ   SEQUENCE   448 AA;  50292 MW;  0AE3DF94FA9A7BD1 CRC64;
     MDRRRFIRNS TIVAGTTILP SGILFARDKG NVKLGYIGVG LRGRNHIKEG LLRDDVEIVA
     ICDTQESSLK LCREQFTKAG KALPKEYTGG LDAYKKLLER KDIDAVIIST PWQFHRDQAV
     DAMNAGKYVG CEVIAGLTVQ DHWDIVNASE KTGIPYMTLE NVCYRRDVMA VLNMVRAGEF
     GELVHLEGGY QHDLRDVLFN DGKNFYGHGV EFGADKSIGE AQWRTQYNID VDGDLYPTHG
     LGPVMNYIDI NRGNRLTNMV SFSSKARGLA DYVNKKSPGH PNAKINYKNG DIVTTLINCA
     NGETISLTHD THLPRPYSIG FRVQGTNGLW MDVAKSIHIE GKSKPHTWDS TKEWFEKYDH
     PLWKKYVDLA QGAGHGGMDW FVFNAFVQAV KQKRQTPIDV YDSVTMSVIF PLSVKSLQEG
     NSSQDIPDFT KGKWKNRKNT FALDDSGF
//
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