MTLD_SHIFL
ID MTLD_SHIFL Reviewed; 382 AA.
AC Q83PQ0; Q7UAY9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00196};
DE EC=1.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00196};
GN Name=mtlD {ECO:0000255|HAMAP-Rule:MF_00196};
GN OrderedLocusNames=SF3634, S4134;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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:0000255|HAMAP-
CC Rule:MF_00196};
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00196}.
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DR EMBL; AE005674; AAN45081.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19108.1; -; Genomic_DNA.
DR RefSeq; NP_709374.2; NC_004337.2.
DR RefSeq; WP_000645424.1; NZ_WPGW01000093.1.
DR PDB; 3H2Z; X-ray; 1.90 A; A=1-382.
DR PDBsum; 3H2Z; -.
DR AlphaFoldDB; Q83PQ0; -.
DR SMR; Q83PQ0; -.
DR STRING; 198214.SF3634; -.
DR EnsemblBacteria; AAN45081; AAN45081; SF3634.
DR EnsemblBacteria; AAP19108; AAP19108; S4134.
DR GeneID; 1023609; -.
DR GeneID; 66672505; -.
DR KEGG; sfl:SF3634; -.
DR KEGG; sfx:S4134; -.
DR PATRIC; fig|198214.7.peg.4291; -.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OrthoDB; 1442117at2; -.
DR EvolutionaryTrace; Q83PQ0; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; 1.10.1040.10; -; 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 Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..382
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000170718"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 44..62
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3H2Z"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 242..263
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 267..281
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 340..362
FT /evidence="ECO:0007829|PDB:3H2Z"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:3H2Z"
SQ SEQUENCE 382 AA; 41139 MW; 0EE8392D33C58CDE CRC64;
MKALHFGAGN IGRGFIGKLL ADAGIQLTFA DVNQVVLDAL NARHSYQVHV VGETEQVDTV
SGVNAVSSIG DDVVDLIAQV DLVTTAVGPV VLERIAPAIA KGLVKRKEQG NESPLNIIAC
ENMVRGTTQL KGHVMNALPE DAKAWVEEHV GFVDSAVDRI VPPSASATND PLEVTVETFS
EWIVDKTQFK GALPNIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL
DEKIRAVVKG AMEESGAVLI KRYGFDADKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK
LSAGDRLIKP LLGTLEYSLP HKNLIQGIAG AMHFRSEDDP QAQELAALIA DKGPQAALAQ
ISGLDANSEV VSEAVTAYKA MQ
