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Conserved domains on  [gi|1750864347|gb|KAA8748768|]
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myo-inosose-2 dehydratase [Priestia megaterium]

Protein Classification

IolE/MocC family protein( domain architecture ID 1001934)

IolE/MocC family similar to Salmonella enterica inosose dehydratase (IolE) and Sinorhizobium meliloti rhizopine catabolism protein MocC

CATH:  3.20.20.150

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
VpdB_C super family cl30226
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
5-293 2.26e-162

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


The actual alignment was detected with superfamily member TIGR04379:

Pssm-ID: 421976  Cd Length: 290  Bit Score: 452.88  E-value: 2.26e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347   5 NILWGIAPIGWRNDDIPEIGAENTLQHLLSDIVVAGFQGTEVGGFFP-EPSILNKELELRNLRIAGQWFSSFIIRDGIEE 83
Cdd:TIGR04379   1 KVKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPrDPAVLRAALEERGLELVSGWYSGLLLTRSVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347  84 TLILFHKHCQYLQEVHADVAVVSEQTYSVQGIERNVFAEKPYFSDQEWEALCAGLNELGKIAAEYGLRLVYHHHMGTGVQ 163
Cdd:TIGR04379  81 EIEAFRPHLEFLKAMGAKVIVVCETGGSIQGDPDTPLSDRPVLTDEEWERLGEGLNRLGEIAAEQGMKLAYHHHMGTVVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 164 TLAEIDRLMEGTDANHVHLLYDTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNVLEQCKREGKSFLQSFLAGMFTVPG 243
Cdd:TIGR04379 161 TEEEIDRLMAMTDPELVGLLYDTGHATFAGGDPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFTVPG 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1750864347 244 DGCVDFTNVYKALVDYNYKGWIVVEAEQDPSIAHPLEYALMARKYINEKL 293
Cdd:TIGR04379 241 DGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
 
Name Accession Description Interval E-value
myo_inos_iolE TIGR04379
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
5-293 2.26e-162

myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]


Pssm-ID: 275172  Cd Length: 290  Bit Score: 452.88  E-value: 2.26e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347   5 NILWGIAPIGWRNDDIPEIGAENTLQHLLSDIVVAGFQGTEVGGFFP-EPSILNKELELRNLRIAGQWFSSFIIRDGIEE 83
Cdd:TIGR04379   1 KVKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPrDPAVLRAALEERGLELVSGWYSGLLLTRSVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347  84 TLILFHKHCQYLQEVHADVAVVSEQTYSVQGIERNVFAEKPYFSDQEWEALCAGLNELGKIAAEYGLRLVYHHHMGTGVQ 163
Cdd:TIGR04379  81 EIEAFRPHLEFLKAMGAKVIVVCETGGSIQGDPDTPLSDRPVLTDEEWERLGEGLNRLGEIAAEQGMKLAYHHHMGTVVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 164 TLAEIDRLMEGTDANHVHLLYDTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNVLEQCKREGKSFLQSFLAGMFTVPG 243
Cdd:TIGR04379 161 TEEEIDRLMAMTDPELVGLLYDTGHATFAGGDPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFTVPG 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1750864347 244 DGCVDFTNVYKALVDYNYKGWIVVEAEQDPSIAHPLEYALMARKYINEKL 293
Cdd:TIGR04379 241 DGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
9-293 3.07e-49

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 164.03  E-value: 3.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347   9 GIAPIGWRNDDIPEIgaentlqhlLSDIVVAGFQGTEVGGFFPE---PSILNKELELRNLRIAGQWFSSFII---RDGIE 82
Cdd:COG1082     4 GLSTYSLPDLDLEEA---------LRAAAELGYDGVELAGGDLDeadLAELRAALADHGLEISSLHAPGLNLapdPEVRE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347  83 ETLILFHKHCQYLQEVHADVAVVSEQTYSVQGIERnvfaekpyfsDQEWEALCAGLNELGKIAAEYGLRLVYHHHMGTGV 162
Cdd:COG1082    75 AALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPP----------EEAWDRLAERLRELAELAEEAGVTLALENHEGTFV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 163 QTLAEIDRLMEGTDANHVHLLYDTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNvleqckregksflqsflagMFTVP 242
Cdd:COG1082   145 NTPEEALRLLEAVDSPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDADGD-------------------QHLPP 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1750864347 243 GDGCVDFTNVYKALVDYNYKGWIVVEAEQDPsiAHPLEYALMARKYINEKL 293
Cdd:COG1082   206 GEGDIDFAAILRALKEAGYDGWLSLEVESDP--DDPEEAARESLEYLRKLL 254
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
58-283 2.01e-23

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 95.90  E-value: 2.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347  58 KELELRNLRIAGqwFSSFIIRDGI-------EETLILFHKHCQYLQEVHADVAVVseqtysVQGIERNVFAEkpyfsdQE 130
Cdd:pfam01261  34 AALKEHGLEIVV--HAPYLGDNLAspdeeerEKAIDRLKRAIELAAALGAKLVVF------HPGSDLGDDPE------EA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 131 WEALCAGLNELGKIAAEYGLRLVYHHHMGTGVQ---TLAEIDRLMEGTDANHVHLLYDTGHIY-VSDGDYMELLHkHIDR 206
Cdd:pfam01261 100 LARLAESLRELADLAEREGVRLALEPLAGKGTNvgnTFEEALEIIDEVDSPNVGVCLDTGHLFaAGDGDLFELRL-GDRY 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750864347 207 IKHVHFKDARRNVLEQCKRegksflqsflagmFTVPGDGCVDFTNVYKALVDYNYKGWIVVEAEQDPSIAHPLEYAL 283
Cdd:pfam01261 179 IGHVHLKDSKNPLGSGPDR-------------HVPIGEGVIDFEALFRALKEIGYDGPLSLETFNDGPPEEGAREGL 242
VpdB_C cd22304
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
168-293 6.29e-10

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


Pssm-ID: 408997  Cd Length: 126  Bit Score: 56.14  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 168 IDRLMEgTDANHVHLLYDTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNVLEQCKREGKSFLQSFLAGmfTVPGDGCV 247
Cdd:cd22304     1 SGRQQE-QSIPKTMLLLSRLQNFKQGDDWSQHVRKTIDRLMLLKGENVRPPITKDQVDLCLQWQEIKSVH--ANPAERLR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1750864347 248 DFTNVYKALV----DYNYKGWIVVEAEQDPSIAHPLEYAlmARKYINEKL 293
Cdd:cd22304    78 EFNYALLISPlvsnQQEINFSKEIRKEIDSLKRLPGLYK--TTKDFTEEF 125
PRK13210 PRK13210
L-ribulose-5-phosphate 3-epimerase;
185-293 3.68e-06

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237308  Cd Length: 284  Bit Score: 47.59  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 185 DTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRnVLEQCKregksflqsflaGMF-TVP-GDGCVDFTNVYKALVDYNYK 262
Cdd:PRK13210  182 DVGNLSAWGNDVWSELKLGIDHIAAIHLKDTYA-VTETSK------------GQFrDVPfGEGCVDFVGIFKTLKELNYR 248
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1750864347 263 GWIVVE--AEQDpsiAHPLEYALMARKYINEKL 293
Cdd:PRK13210  249 GPFLIEmwTEKA---EEPRAEIKQARRFLEPLM 278
 
Name Accession Description Interval E-value
myo_inos_iolE TIGR04379
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
5-293 2.26e-162

myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]


Pssm-ID: 275172  Cd Length: 290  Bit Score: 452.88  E-value: 2.26e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347   5 NILWGIAPIGWRNDDIPEIGAENTLQHLLSDIVVAGFQGTEVGGFFP-EPSILNKELELRNLRIAGQWFSSFIIRDGIEE 83
Cdd:TIGR04379   1 KVKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPrDPAVLRAALEERGLELVSGWYSGLLLTRSVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347  84 TLILFHKHCQYLQEVHADVAVVSEQTYSVQGIERNVFAEKPYFSDQEWEALCAGLNELGKIAAEYGLRLVYHHHMGTGVQ 163
Cdd:TIGR04379  81 EIEAFRPHLEFLKAMGAKVIVVCETGGSIQGDPDTPLSDRPVLTDEEWERLGEGLNRLGEIAAEQGMKLAYHHHMGTVVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 164 TLAEIDRLMEGTDANHVHLLYDTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNVLEQCKREGKSFLQSFLAGMFTVPG 243
Cdd:TIGR04379 161 TEEEIDRLMAMTDPELVGLLYDTGHATFAGGDPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFTVPG 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1750864347 244 DGCVDFTNVYKALVDYNYKGWIVVEAEQDPSIAHPLEYALMARKYINEKL 293
Cdd:TIGR04379 241 DGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
9-293 3.07e-49

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 164.03  E-value: 3.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347   9 GIAPIGWRNDDIPEIgaentlqhlLSDIVVAGFQGTEVGGFFPE---PSILNKELELRNLRIAGQWFSSFII---RDGIE 82
Cdd:COG1082     4 GLSTYSLPDLDLEEA---------LRAAAELGYDGVELAGGDLDeadLAELRAALADHGLEISSLHAPGLNLapdPEVRE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347  83 ETLILFHKHCQYLQEVHADVAVVSEQTYSVQGIERnvfaekpyfsDQEWEALCAGLNELGKIAAEYGLRLVYHHHMGTGV 162
Cdd:COG1082    75 AALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPP----------EEAWDRLAERLRELAELAEEAGVTLALENHEGTFV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 163 QTLAEIDRLMEGTDANHVHLLYDTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNvleqckregksflqsflagMFTVP 242
Cdd:COG1082   145 NTPEEALRLLEAVDSPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDADGD-------------------QHLPP 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1750864347 243 GDGCVDFTNVYKALVDYNYKGWIVVEAEQDPsiAHPLEYALMARKYINEKL 293
Cdd:COG1082   206 GEGDIDFAAILRALKEAGYDGWLSLEVESDP--DDPEEAARESLEYLRKLL 254
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
58-283 2.01e-23

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 95.90  E-value: 2.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347  58 KELELRNLRIAGqwFSSFIIRDGI-------EETLILFHKHCQYLQEVHADVAVVseqtysVQGIERNVFAEkpyfsdQE 130
Cdd:pfam01261  34 AALKEHGLEIVV--HAPYLGDNLAspdeeerEKAIDRLKRAIELAAALGAKLVVF------HPGSDLGDDPE------EA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 131 WEALCAGLNELGKIAAEYGLRLVYHHHMGTGVQ---TLAEIDRLMEGTDANHVHLLYDTGHIY-VSDGDYMELLHkHIDR 206
Cdd:pfam01261 100 LARLAESLRELADLAEREGVRLALEPLAGKGTNvgnTFEEALEIIDEVDSPNVGVCLDTGHLFaAGDGDLFELRL-GDRY 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750864347 207 IKHVHFKDARRNVLEQCKRegksflqsflagmFTVPGDGCVDFTNVYKALVDYNYKGWIVVEAEQDPSIAHPLEYAL 283
Cdd:pfam01261 179 IGHVHLKDSKNPLGSGPDR-------------HVPIGEGVIDFEALFRALKEIGYDGPLSLETFNDGPPEEGAREGL 242
VpdB_C cd22304
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
168-293 6.29e-10

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


Pssm-ID: 408997  Cd Length: 126  Bit Score: 56.14  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 168 IDRLMEgTDANHVHLLYDTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNVLEQCKREGKSFLQSFLAGmfTVPGDGCV 247
Cdd:cd22304     1 SGRQQE-QSIPKTMLLLSRLQNFKQGDDWSQHVRKTIDRLMLLKGENVRPPITKDQVDLCLQWQEIKSVH--ANPAERLR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1750864347 248 DFTNVYKALV----DYNYKGWIVVEAEQDPSIAHPLEYAlmARKYINEKL 293
Cdd:cd22304    78 EFNYALLISPlvsnQQEINFSKEIRKEIDSLKRLPGLYK--TTKDFTEEF 125
Hyi COG3622
Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and ...
131-265 2.47e-07

Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and metabolism];


Pssm-ID: 442840  Cd Length: 260  Bit Score: 50.88  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 131 WEALCAGLNELGKIAAEYGLRLV-----------YH-HHMGtgvQTLAEIDRLmegtDANHVHLLYDTGHIYVSDGDYME 198
Cdd:COG3622   119 LATFVENLRYAADLAAPHGITLLieplnsrdhpgYFlDTTA---QAVAIIEAV----GSPNLKLLYDIYHMQIMEGDLIR 191
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864347 199 LLHKHIDRIKHVHFKDA-RRNvlEqckregksflqsflagmftvPGDGCVDFTNVYKALVDYNYKGWI 265
Cdd:COG3622   192 TIRRHLPRIGHVQIADVpGRH--E--------------------PGTGELNYPAIFKALDALGYDGWV 237
PRK13210 PRK13210
L-ribulose-5-phosphate 3-epimerase;
185-293 3.68e-06

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237308  Cd Length: 284  Bit Score: 47.59  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 185 DTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRnVLEQCKregksflqsflaGMF-TVP-GDGCVDFTNVYKALVDYNYK 262
Cdd:PRK13210  182 DVGNLSAWGNDVWSELKLGIDHIAAIHLKDTYA-VTETSK------------GQFrDVPfGEGCVDFVGIFKTLKELNYR 248
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1750864347 263 GWIVVE--AEQDpsiAHPLEYALMARKYINEKL 293
Cdd:PRK13210  249 GPFLIEmwTEKA---EEPRAEIKQARRFLEPLM 278
PRK13209 PRK13209
L-ribulose-5-phosphate 3-epimerase;
183-294 9.77e-04

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237307  Cd Length: 283  Bit Score: 39.97  E-value: 9.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864347 183 LY-DTGHIYVSDGDYMELLHKHIDRIKHVHFKDARRNVLEQckregksflqsflagmftVP-GDGCVDFTNVYKALVDYN 260
Cdd:PRK13209  184 LYpDIGNLSAWDNDVQMELQAGIGHIVAFHVKDTKPGVFKN------------------VPfGEGVVDFERCFKTLKQSG 245
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1750864347 261 YKGWIVVEAEQDpSIAHPLEYALMARKYINEKLV 294
Cdd:PRK13209  246 YCGPYLIEMWSE-TAEDPAAEVAKARDFVKARMA 278
 
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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