MTLD_PSECP
ID MTLD_PSECP Reviewed; 387 AA.
AC B8H7T9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
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}; OrderedLocusNames=Achl_3788;
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC 13794 / A6;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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; 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; CP001341; ACL41742.1; -; Genomic_DNA.
DR RefSeq; WP_015938935.1; NC_011886.1.
DR AlphaFoldDB; B8H7T9; -.
DR SMR; B8H7T9; -.
DR STRING; 452863.Achl_3788; -.
DR EnsemblBacteria; ACL41742; ACL41742; Achl_3788.
DR KEGG; ach:Achl_3788; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_0_1_11; -.
DR OMA; GKKAVHF; -.
DR OrthoDB; 1442117at2; -.
DR Proteomes; UP000002505; 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; 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.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..387
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000124383"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 387 AA; 40718 MW; 0B57EEC1CC7684C7 CRC64;
MKAVHFGAGN IGRGFVGLLL HNAGYEVVFA DVAEGLIAQL ADADSYAVHE VGESPAVQTV
DNFRALNSNT QEAELITEIA TADIVTTAVG PHILKFVAPV IARGIAARGA GMAPLQVMAC
ENAINATDVL AREVASRPEA AGGALDGQAV FANTAVDRIV PNQEAGQGLD VTVESFYEWV
IDRTAFAGSE PEIPGATFVD ELAPYIERKL FTVNTGHASA AYFGFEAGLE KISDAMADQD
VAEDVRAVLE ETKQLLVAKH GFSNEAQEAY VQKILVRFTN PHLPDTVNRV GRAPLRKLSR
HERFIGPAAE LAERGVVPEA LLGAISAALR FTDPADAEAT ELAGILASGS AADATARITG
LDPDHPLFNA VSTLVEERQA ELAATSA