ID   M1PD_ALIF1              Reviewed;         423 AA.
AC   Q5E1G4;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000303|PubMed:28446608};
DE            EC=1.1.1.17 {ECO:0000305|PubMed:28446608};
GN   Name=yggP {ECO:0000312|EMBL:AAW87132.1};
GN   OrderedLocusNames=VF_A0062 {ECO:0000312|EMBL:AAW87132.1};
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=28446608; DOI=10.1074/jbc.m116.763193;
RA   Pan S., Nikolakakis K., Adamczyk P.A., Pan M., Ruby E.G., Reed J.L.;
RT   "Model-enabled gene search (MEGS) allows fast and direct discovery of
RT   enzymatic and transport gene functions in the marine bacterium Vibrio
RT   fischeri.";
RL   J. Biol. Chem. 292:10250-10261(2017).
CC   -!- FUNCTION: Seems to be involved in mannitol utilization. Complements an
CC       E. coli mtlD deletion mutant. {ECO:0000269|PubMed:28446608}.
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:0000305|PubMed:28446608};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O58389};
CC   -!- INDUCTION: Induced by mannitol. {ECO:0000269|PubMed:28446608}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant cannot grow in minimal medium.
CC       Mutant fails to persist in the squid. {ECO:0000269|PubMed:28446608}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000021; AAW87132.1; -; Genomic_DNA.
DR   RefSeq; WP_011262964.1; NC_006841.2.
DR   RefSeq; YP_206020.1; NC_006841.2.
DR   AlphaFoldDB; Q5E1G4; -.
DR   SMR; Q5E1G4; -.
DR   STRING; 312309.VF_A0062; -.
DR   EnsemblBacteria; AAW87132; AAW87132; VF_A0062.
DR   KEGG; vfi:VF_A0062; -.
DR   PATRIC; fig|312309.11.peg.2666; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_054732_0_0_6; -.
DR   OMA; LNFYNVH; -.
DR   OrthoDB; 972769at2; -.
DR   Proteomes; UP000000537; Chromosome II.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..423
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000440875"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O58389"
SQ   SEQUENCE   423 AA;  45716 MW;  F57BD7E5E1BD8061 CRC64;
     MTQTTAAVIC GEKDIQLRTF ELPSISADEL LVKNISNSVC LSTYKAALLG SKHKRVPENI
     DEVPVITGHE YAGVIVEVGE NLKDQFKAGD SFVLQPAMGL PTGYSAGYSY ETFGGNATYS
     IIPKIAIDLG CVLPYDGSYY ADASLAEPMS CIIGAFHASY HTTQFVYEHE MGIKEGGTLA
     LLACAGPMGI GAIDYAINGP VKPRRIVVTD IDEDRLSRAE SLIPVSAAKA QGIELIYVNT
     IEMEDPVTYL KSLNDDQGYD DVMVYAAVAQ VLEQADALLG NDGCLNFFAG PTDKEFKVPF
     NFYNVHYEST HIVGTSGGST GDMVESLELS AQGDINPSFM ITHVGGLQAA PHTILNQLDI
     PGGKKLIYPH IDLPLTAIDN FASLAEQDPF FSELDAILAK NNYVWNQHAE KALLEFYDVS
     LSV