ID A0A0K8JD26_9FIRM Unreviewed; 385 AA.
AC A0A0K8JD26;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=P22_1278 {ECO:0000313|EMBL:CUH95208.1};
OS Propionispora sp. 2/2-37.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH95208.1, ECO:0000313|Proteomes:UP000041641};
RN [1] {ECO:0000313|EMBL:CUH95208.1, ECO:0000313|Proteomes:UP000041641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2/2 {ECO:0000313|EMBL:CUH95208.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000292};
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DR EMBL; CYSP01000005; CUH95208.1; -; Genomic_DNA.
DR RefSeq; WP_054259395.1; NZ_CYSP01000005.1.
DR AlphaFoldDB; A0A0K8JD26; -.
DR STRING; 1677858.P22_1278; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000041641; 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; IPR000669; Mannitol_DH.
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 PRINTS; PR00084; MTLDHDRGNASE.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000041641}.
FT DOMAIN 1..123
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 151..354
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 385 AA; 43214 MW; 19755F2257D5F108 CRC64;
MKAVHFGAGS IGRGFIADLL HDSGYDIVFL DVDDHLINQI NHTGTYNLYL INEHFSKKTI
NQVKAISSLS NEKEAIEEIR TADLITTSVW ADNLPKIAPI LVKGLKERRK TKAAKINLLA
CENALFNSEI LKREILKIAD GFTESDLNEV AAFPNTAVDR LVLEAVRDGE RVIDIGSEHE
LVIERNKLAD PGIEPIKGAV YTDNLQKYIE RKLYIINCGH AWAGYMGHIY GYTGMQDIFH
NEQLVSGVRE VMLESSGLLA QKYDFSLEDL KAYIEFAIAR FQTPGITDTV NRVARSPIRK
LQQNERLTGP CIQCEEYGLQ NSRLLQGIAA AFLFNNPADE QSAALQYHIK KYGIAESIPF
YTAIPADSRM YAVILEQYGS LKNYH
//
