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Conserved domains on  [gi|52698198|gb|AAU86836|]
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mannitol-1-phosphate dehydrogenase, partial [Shigella flexneri]

Protein Classification

mannitol-1-phosphate 5-dehydrogenase( domain architecture ID 11479775)

mannitol-1-phosphate 5-dehydrogenase catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway

EC:  1.1.1.17
Gene Ontology:  GO:0008926|GO:0019594
PubMed:  14367396

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-213 8.67e-133

mannitol-1-phosphate 5-dehydrogenase; Provisional


:

Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 378.01  E-value: 8.67e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198    1 IGRGFIGKLLADAGIQLTFADVNQVVLDALNARHSYQVHVVGETEQVDTVSGVNAVSSIG-DDVVDLIAQVDLVTTAVGP 79
Cdd:PRK02318  11 IGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADeEAVIEAIAEADLVTTAVGP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198   80 VVLERIAPAIAKGLVKRKEQGNESPLNIIACENMVRGTTQLKGHVMNALPEDAKAWVEEHVGFVDSAVDRIVPpsASATN 159
Cdd:PRK02318  91 NILPFIAPLIAKGLKKRKAQGNTKPLNIIACENMIRGTSFLKKHVLKALSEDEKAWLEEHVGFVDSAVDRIVP--AQKNE 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 52698198  160 DPLEVTVETFSEWIVDKTQFKGALPNIPSMELTDNLMAFVERKLFTLNTGHAIT 213
Cdd:PRK02318 169 DPLDVTVEPFSEWIVDKTQFKGALPKIKGMEYVDNLMPFIERKLFTVNTGHATT 222
 
Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-213 8.67e-133

mannitol-1-phosphate 5-dehydrogenase; Provisional


Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 378.01  E-value: 8.67e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198    1 IGRGFIGKLLADAGIQLTFADVNQVVLDALNARHSYQVHVVGETEQVDTVSGVNAVSSIG-DDVVDLIAQVDLVTTAVGP 79
Cdd:PRK02318  11 IGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADeEAVIEAIAEADLVTTAVGP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198   80 VVLERIAPAIAKGLVKRKEQGNESPLNIIACENMVRGTTQLKGHVMNALPEDAKAWVEEHVGFVDSAVDRIVPpsASATN 159
Cdd:PRK02318  91 NILPFIAPLIAKGLKKRKAQGNTKPLNIIACENMIRGTSFLKKHVLKALSEDEKAWLEEHVGFVDSAVDRIVP--AQKNE 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 52698198  160 DPLEVTVETFSEWIVDKTQFKGALPNIPSMELTDNLMAFVERKLFTLNTGHAIT 213
Cdd:PRK02318 169 DPLDVTVEPFSEWIVDKTQFKGALPKIKGMEYVDNLMPFIERKLFTVNTGHATT 222
Mannitol_dh_C pfam08125
Mannitol dehydrogenase C-terminal domain;
138-213 2.98e-26

Mannitol dehydrogenase C-terminal domain;


Pssm-ID: 369700  Cd Length: 246  Bit Score: 101.30  E-value: 2.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198   138 EHVGFVDSAVDRIVPPS----------ASATNDPLEVTVETFSEWIVDKTQFKG-ALPNIPSMELTDNLMAFVERKLFTL 206
Cdd:pfam08125   1 DNVGFPNTMVDRIVPATtddelakiaqALGVEDPLPVTVEPFRQWVIEDNFVKGrPLLEKVGVEYVEDVDPYEERKLRIL 80

                  ....*..
gi 52698198   207 NTGHAIT 213
Cdd:pfam08125  81 NGGHATL 87
MtlD COG0246
Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];
88-210 2.12e-11

Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];


Pssm-ID: 440016 [Multi-domain]  Cd Length: 492  Bit Score: 62.09  E-value: 2.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198  88 AIAKGLVKRKEQGnESPLNIIACENMVRGTTQLKGHVM---NALPEDAKAWVEEHVGFVDSAVDRIVPPSASAT------ 158
Cdd:COG0246 167 KLTAALYRRRAAG-LKPFTVLSCDNLPHNGDVLREAVLafaRLWDPELADWIEENVTFPNTMVDRIVPATTDEDrarlaa 245
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198 159 ----NDPLEVTVETFSEWIVDKTQFKGALP----NIpsmELTDNLMAFVERKLFTLNTGH 210
Cdd:COG0246 246 elgyEDAAPVVAEPFRQWVIEDDFPAGRPPlekaGV---QFVDDVAPYEEMKLRLLNGSH 302
 
Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-213 8.67e-133

mannitol-1-phosphate 5-dehydrogenase; Provisional


Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 378.01  E-value: 8.67e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198    1 IGRGFIGKLLADAGIQLTFADVNQVVLDALNARHSYQVHVVGETEQVDTVSGVNAVSSIG-DDVVDLIAQVDLVTTAVGP 79
Cdd:PRK02318  11 IGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADeEAVIEAIAEADLVTTAVGP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198   80 VVLERIAPAIAKGLVKRKEQGNESPLNIIACENMVRGTTQLKGHVMNALPEDAKAWVEEHVGFVDSAVDRIVPpsASATN 159
Cdd:PRK02318  91 NILPFIAPLIAKGLKKRKAQGNTKPLNIIACENMIRGTSFLKKHVLKALSEDEKAWLEEHVGFVDSAVDRIVP--AQKNE 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 52698198  160 DPLEVTVETFSEWIVDKTQFKGALPNIPSMELTDNLMAFVERKLFTLNTGHAIT 213
Cdd:PRK02318 169 DPLDVTVEPFSEWIVDKTQFKGALPKIKGMEYVDNLMPFIERKLFTVNTGHATT 222
Mannitol_dh_C pfam08125
Mannitol dehydrogenase C-terminal domain;
138-213 2.98e-26

Mannitol dehydrogenase C-terminal domain;


Pssm-ID: 369700  Cd Length: 246  Bit Score: 101.30  E-value: 2.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198   138 EHVGFVDSAVDRIVPPS----------ASATNDPLEVTVETFSEWIVDKTQFKG-ALPNIPSMELTDNLMAFVERKLFTL 206
Cdd:pfam08125   1 DNVGFPNTMVDRIVPATtddelakiaqALGVEDPLPVTVEPFRQWVIEDNFVKGrPLLEKVGVEYVEDVDPYEERKLRIL 80

                  ....*..
gi 52698198   207 NTGHAIT 213
Cdd:pfam08125  81 NGGHATL 87
Mannitol_dh pfam01232
Mannitol dehydrogenase Rossmann domain;
1-113 7.92e-24

Mannitol dehydrogenase Rossmann domain;


Pssm-ID: 395986 [Multi-domain]  Cd Length: 151  Bit Score: 92.47  E-value: 7.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198     1 IGRG---FIGKLLADAGIQLTFADVNQVVLDA---LNARHSYQVHVVG--ETEQVDTVSGVNAVSSIGDDVVDLIA---- 68
Cdd:pfam01232  11 FHRAhqaFIGDLLAENGFDWGIVDVNLRVVDAreaLNAQDGLYTVIEDgeEGRQARLVGSVNAVNSVEEDLEALIElmae 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52698198    69 -QVDLVTTAVGP----------VVLERIAPAIAKG-----LVKRKEQGNESPLNIIACENM 113
Cdd:pfam01232  91 pQADIVSTTVTEggidatgqldNDLPDIAADLAKPeylveALKRRRAAGLKPLTIIACDNM 151
MtlD COG0246
Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];
88-210 2.12e-11

Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];


Pssm-ID: 440016 [Multi-domain]  Cd Length: 492  Bit Score: 62.09  E-value: 2.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198  88 AIAKGLVKRKEQGnESPLNIIACENMVRGTTQLKGHVM---NALPEDAKAWVEEHVGFVDSAVDRIVPPSASAT------ 158
Cdd:COG0246 167 KLTAALYRRRAAG-LKPFTVLSCDNLPHNGDVLREAVLafaRLWDPELADWIEENVTFPNTMVDRIVPATTDEDrarlaa 245
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198 159 ----NDPLEVTVETFSEWIVDKTQFKGALP----NIpsmELTDNLMAFVERKLFTLNTGH 210
Cdd:COG0246 246 elgyEDAAPVVAEPFRQWVIEDDFPAGRPPlekaGV---QFVDDVAPYEEMKLRLLNGSH 302
PRK03643 PRK03643
tagaturonate reductase;
88-210 5.50e-10

tagaturonate reductase;


Pssm-ID: 235147 [Multi-domain]  Cd Length: 471  Bit Score: 57.93  E-value: 5.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198   88 AIAKGLVkrkeqgnesplnIIACENMVRGTTQLKGHVM-----NALPEDAKAWVEEHVGFVDSAVDRIVP--PSASATN- 159
Cdd:PRK03643 159 AADKGLI------------IIPCELIDYNGEKLKEIVLryaqeWNLPEAFIQWLEEANTFCSTLVDRIVTgyPRDEAAAl 226
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52698198  160 -------DPLEVTVETF-------SEWIVDKTQFKGALPNIpsmELTDNLMAFVERKLFTLNTGH 210
Cdd:PRK03643 227 eeelgyeDGLLDTAEPFylwviegPKSLAKELPFDKAGLNV---LIVDDIKPYRERKVRILNGAH 288
PRK15037 PRK15037
D-mannonate oxidoreductase; Provisional
89-211 1.24e-07

D-mannonate oxidoreductase; Provisional


Pssm-ID: 184997 [Multi-domain]  Cd Length: 486  Bit Score: 51.19  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52698198   89 IAKGLVKRKEQGNESpLNIIACENMVRGTTQLKGHVMN-ALPEDAK--AWVEEHVGFVDSAVDRIVPPSASAT------- 158
Cdd:PRK15037 165 IVEALRLRREKGLKA-FTVMSCDNVRENGHVAKVAVLGlAQARDPQlaAWIEENVTFPCTMVDRIVPAATPETlqeiadq 243
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 52698198  159 ---NDPLEVTVETFSEWIVDKtQFKGALPNIPSM--ELTDNLMAFVERKLFTLNTGHA 211
Cdd:PRK15037 244 lgvYDPCAIACEPFRQWVIED-NFVNGRPDWDKVgaQFVADVVPFEMMKLRMLNGSHS 300
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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