ID A0A1H6SXW2_9BACT Unreviewed; 511 AA.
AC A0A1H6SXW2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Tagaturonate reductase {ECO:0000313|EMBL:SEI72621.1};
GN ORFNames=SAMN05216327_103453 {ECO:0000313|EMBL:SEI72621.1};
OS Dyadobacter sp. SG02.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1855291 {ECO:0000313|EMBL:SEI72621.1, ECO:0000313|Proteomes:UP000199631};
RN [1] {ECO:0000313|EMBL:SEI72621.1, ECO:0000313|Proteomes:UP000199631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG02 {ECO:0000313|EMBL:SEI72621.1,
RC ECO:0000313|Proteomes:UP000199631};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNYL01000003; SEI72621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6SXW2; -.
DR STRING; 1855291.SAMN05216327_103453; -.
DR OrthoDB; 9768714at2; -.
DR Proteomes; UP000199631; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 31..144
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 219..475
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 511 AA; 58165 MW; 2BAB365D0F8A0998 CRC64;
MGYLFRENLR QLRSQPAVVV ADDSVFQLPE KVLQFGTGAF LRGLADYFID KANRQGVFNG
RIVVVKSTDQ GDTKAFERQD NLYTICSRGI QNGEAKEENI ISSAISRVLS AKTQWSLVLD
LAKNPAVSIV ISNTTETGIQ LVQDDIYQWP PVSFPGKLLA FLYARYVAFS GNPDFGITII
PTELIADNGK KLESIILELA HRNGLEGAFI DWIEQCNFFC NSLVDRIVPG KPDEIRLKEL
EEELGYRDEL LIATEHYHLW AIEGDERIRQ KIGFYGIDEG LIIEPDIEQY RELKLRLLNG
PHTLGGGLAH LCGFKTVVEA MNDPFFSAYI THLMESEIAT SIPYDVRPEV ALAFSRQVAD
RFRNPHILHK WFNINQNYSA KILSRVIPTY LNYEAKNGYL PEYMTFGLAV FIHFMKVVKK
EGDHYYGRIE GVPYLIQDPK APFFYQKWQM ASLPDMVQAI LKEQSIWGRD LNKIDSVHSS
IVRYLQSIAQ IGITETLKTL LEKTEYALSQ S
//