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Database: UniProt
Entry: F4HF13_GALAU
LinkDB: F4HF13_GALAU
Original site: F4HF13_GALAU 
ID   F4HF13_GALAU            Unreviewed;       384 AA.
AC   F4HF13;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219, ECO:0000256|HAMAP-Rule:MF_00196};
DE            EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939, ECO:0000256|HAMAP-Rule:MF_00196};
GN   Name=mtlD {ECO:0000256|HAMAP-Rule:MF_00196};
GN   OrderedLocusNames=UMN179_00905 {ECO:0000313|EMBL:AEC16933.1};
OS   Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Gallibacterium.
OX   NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC16933.1, ECO:0000313|Proteomes:UP000006908};
RN   [1] {ECO:0000313|EMBL:AEC16933.1, ECO:0000313|Proteomes:UP000006908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN179 {ECO:0000313|EMBL:AEC16933.1,
RC   ECO:0000313|Proteomes:UP000006908};
RX   PubMed=21602325; DOI=10.1128/JB.05177-11;
RA   Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA   Seemann T.;
RT   "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT   from a laying hen with peritonitis.";
RL   J. Bacteriol. 193:3676-3677(2011).
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00196};
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00196}.
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DR   EMBL; CP002667; AEC16933.1; -; Genomic_DNA.
DR   RefSeq; WP_013745719.1; NC_015460.1.
DR   AlphaFoldDB; F4HF13; -.
DR   STRING; 1005058.UMN179_00905; -.
DR   KEGG; gan:UMN179_00905; -.
DR   PATRIC; fig|1005058.3.peg.891; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; APFIERK; -.
DR   Proteomes; UP000006908; Chromosome.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR   InterPro; IPR000669; Mannitol_DH.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR023027; Mannitol_DH_CS.
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.
DR   PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00196};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00196}.
FT   DOMAIN          1..125
FT                   /note="Mannitol dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01232"
FT   DOMAIN          151..367
FT                   /note="Mannitol dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08125"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   384 AA;  42622 MW;  97E62F7A3CE3D869 CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGIYVTFA DINETVINQL NQQKSYSVKV VGDGQNKIEI
     VKNVDGINSA NQQQLFEKIQ QVDLITTAIG AGVLKIIAKS LAQGLLQRIQ NGNHQPLNII
     ACENMVRGTS ALKEHVYSHL SEAEQQLIEK YVGFVDSAVD RIVPPVEANS EDPLQVTVEE
     FSEWIVDETQ FKGDIPNIPG MERTDNLMAF IERKLFTLNT GHAVTAYLGK LAGYQFVKQS
     IDDENIKQQV KTVMQESGAV LIKRYQFDPA AHAAYIEKIL KRFANPYLTD DVDRVGREPI
     RKLGYNDRLI KPLRGTLEYQ LPHPMLCKAI AAALCYTNAN DPQAVELQKS IADQGITKTL
     EKYTGLDNTA IFAEIAQNYA SLKK
//
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