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Conserved domains on  [gi|446115538|ref|WP_000193393|]
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MULTISPECIES: shikimate kinase AroL [Enterobacteriaceae]

Protein Classification

shikimate kinase( domain architecture ID 10792322)

shikimate kinase catalyzes the specific phosphorylation of the 3-hydroxylgroup of shikimic acid using ATP as a cosubstrate

EC:  2.7.1.71

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
aroL PRK03731
shikimate kinase AroL;
1-170 1.40e-109

shikimate kinase AroL;


:

Pssm-ID: 235153 [Multi-domain]  Cd Length: 171  Bit Score: 309.57  E-value: 1.40e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   1 MTQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPSTVIATGGG 80
Cdd:PRK03731   1 MTQPLFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAALEAVTAPSTVIATGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  81 IILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQV 160
Cdd:PRK03731  81 IILTEENRHFMRNNGIVIYLCAPVSVLANRLEANPEEDQRPTLTGKPISEEVAEVLAEREALYREVAHHIIDATQPPSQV 160

                        170
                 ....*....|
gi 446115538 161 ISEIRSALAQ 170
Cdd:PRK03731 161 VSEILSALAQ 170
 
Name Accession Description Interval E-value
aroL PRK03731
shikimate kinase AroL;
1-170 1.40e-109

shikimate kinase AroL;


Pssm-ID: 235153 [Multi-domain]  Cd Length: 171  Bit Score: 309.57  E-value: 1.40e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   1 MTQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPSTVIATGGG 80
Cdd:PRK03731   1 MTQPLFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAALEAVTAPSTVIATGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  81 IILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQV 160
Cdd:PRK03731  81 IILTEENRHFMRNNGIVIYLCAPVSVLANRLEANPEEDQRPTLTGKPISEEVAEVLAEREALYREVAHHIIDATQPPSQV 160

                        170
                 ....*....|
gi 446115538 161 ISEIRSALAQ 170
Cdd:PRK03731 161 VSEILSALAQ 170
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 5-170 2.98e-63

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 191.88  E-value: 2.98e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTA-PSTVIATGGGIIL 83
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  84 TEFNRHFMQNNGIVVYLCAPVSVLVNRLQAApeeDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATN-EPSQVIS 162
Cdd:COG0703   81 SPENRELLKEHGTVVYLDASPETLLERLRRD---DNRPLLQGEDPRERLEELLAEREPLYREVADITVDTDGrSPEEVVD 157


                 ....*...
gi 446115538 163 EIRSALAQ 170
Cdd:COG0703  158 EILEALEE 165
SKI pfam01202
Shikimate kinase;
11-169 6.28e-57

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 175.85  E-value: 6.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   11 RGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTA-PSTVIATGGGIILTEFNRH 89
Cdd:pfam01202   1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAeHGLVIATGGGAVLSEENRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   90 FMQNNGIVVYLCAPVSVLVNRLQAAPEedlRPTLTGKPLSEEVQEVL-EERDALYREVAHIIIDATNE-PSQVISEIRSA 167
Cdd:pfam01202  81 LLKERGIVIYLDAPLEVLLERLKRDKT---RPLLQNKDPEEELLELLfEERDPLYEEAADIVIDTDESsPEEVATEILEA 157


                  ..
gi 446115538  168 LA 169
Cdd:pfam01202 158 LE 159
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 4-157 2.16e-53

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 166.58  E-value: 2.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   4 PLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAAL-EAVTAPSTVIATGGGII 82
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLlLLLTKENAVIATGGGAV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115538  83 LTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAapeEDLRPTLTGKPlSEEVQEVLEERDALYREVAHIIIDATNEP 157
Cdd:cd00464   81 LREENRRLLLENGIVVWLDASPEELLERLAR---DKTRPLLQDED-PERLRELLEEREPLYREVADLTIDTDELS 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-61 2.57e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 2.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115538     3 QPLFLIGPRGCGKTTVGMALADSLNRR-----FVDTDQWLQSQLNMTVAEIVEREEWAGFRARE 61
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPgggviYIDGEDILEEVLDQLLLIIVGGKKASGSGELR 66
 
Name Accession Description Interval E-value
aroL PRK03731
shikimate kinase AroL;
1-170 1.40e-109

shikimate kinase AroL;


Pssm-ID: 235153 [Multi-domain]  Cd Length: 171  Bit Score: 309.57  E-value: 1.40e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   1 MTQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPSTVIATGGG 80
Cdd:PRK03731   1 MTQPLFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAALEAVTAPSTVIATGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  81 IILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQV 160
Cdd:PRK03731  81 IILTEENRHFMRNNGIVIYLCAPVSVLANRLEANPEEDQRPTLTGKPISEEVAEVLAEREALYREVAHHIIDATQPPSQV 160

                        170
                 ....*....|
gi 446115538 161 ISEIRSALAQ 170
Cdd:PRK03731 161 VSEILSALAQ 170
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 5-170 2.98e-63

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 191.88  E-value: 2.98e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTA-PSTVIATGGGIIL 83
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  84 TEFNRHFMQNNGIVVYLCAPVSVLVNRLQAApeeDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATN-EPSQVIS 162
Cdd:COG0703   81 SPENRELLKEHGTVVYLDASPETLLERLRRD---DNRPLLQGEDPRERLEELLAEREPLYREVADITVDTDGrSPEEVVD 157


                 ....*...
gi 446115538 163 EIRSALAQ 170
Cdd:COG0703  158 EILEALEE 165
SKI pfam01202
Shikimate kinase;
11-169 6.28e-57

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 175.85  E-value: 6.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   11 RGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTA-PSTVIATGGGIILTEFNRH 89
Cdd:pfam01202   1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAeHGLVIATGGGAVLSEENRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   90 FMQNNGIVVYLCAPVSVLVNRLQAAPEedlRPTLTGKPLSEEVQEVL-EERDALYREVAHIIIDATNE-PSQVISEIRSA 167
Cdd:pfam01202  81 LLKERGIVIYLDAPLEVLLERLKRDKT---RPLLQNKDPEEELLELLfEERDPLYEEAADIVIDTDESsPEEVATEILEA 157


                  ..
gi 446115538  168 LA 169
Cdd:pfam01202 158 LE 159
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 4-157 2.16e-53

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 166.58  E-value: 2.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   4 PLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAAL-EAVTAPSTVIATGGGII 82
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLlLLLTKENAVIATGGGAV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115538  83 LTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAapeEDLRPTLTGKPlSEEVQEVLEERDALYREVAHIIIDATNEP 157
Cdd:cd00464   81 LREENRRLLLENGIVVWLDASPEELLERLAR---DKTRPLLQDED-PERLRELLEEREPLYREVADLTIDTDELS 151
aroK PRK00131
shikimate kinase; Reviewed
 5-170 1.50e-52

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 165.36  E-value: 1.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTA-PSTVIATGGGIIL 83
Cdd:PRK00131   7 IVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLArHNLVISTGGGAVL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  84 TEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEedlRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNE-PSQVIS 162
Cdd:PRK00131  87 REENRALLRERGTVVYLDASFEELLRRLRRDRN---RPLLQTNDPKEKLRDLYEERDPLYEEVADITVETDGRsPEEVVN 163


                 ....*...
gi 446115538 163 EIRSALAQ 170
Cdd:PRK00131 164 EILEKLEA 171
aroK PRK05057
shikimate kinase AroK;
5-161 1.49e-28

shikimate kinase AroK;


Pssm-ID: 235335 [Multi-domain]  Cd Length: 172  Bit Score: 104.02  E-value: 1.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEI--VEREEwaGFRARETAALEAVTAPS-TVIATGGGI 81
Cdd:PRK05057   7 IFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVfdVEGEE--GFRDREEKVINELTEKQgIVLATGGGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  82 ILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQaapEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQVI 161
Cdd:PRK05057  85 VKSRETRNRLSARGVVVYLETTIEKQLARTQ---RDKKRPLLQVDDPREVLEALANERNPLYEEIADVTIRTDDQSAKVV 161
PRK13949 PRK13949
shikimate kinase; Provisional
 4-153 1.31e-25

shikimate kinase; Provisional


Pssm-ID: 140006 [Multi-domain]  Cd Length: 169  Bit Score: 96.34  E-value: 1.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   4 PLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTA-PSTVIATGGGII 82
Cdd:PRK13949   3 RIFLVGYMGAGKTTLGKALARELGLSFIDLDFFIENRFHKTVGDIFAERGEAVFRELERNMLHEVAEfEDVVISTGGGAP 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115538  83 LTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEdlRPTLTGKP---LSEEVQEVLEERDALYREvAHIIIDA 153
Cdd:PRK13949  83 CFFDNMELMNASGTTVYLKVSPEVLFVRLRLAKQQ--RPLLKGKSdeeLLDFIIEALEKRAPFYRQ-AKIIFNA 153
PRK13947 PRK13947
shikimate kinase; Provisional
 7-164 2.81e-25

shikimate kinase; Provisional


Pssm-ID: 184412 [Multi-domain]  Cd Length: 171  Bit Score: 95.54  E-value: 2.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   7 LIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPST-VIATGGGIILTE 85
Cdd:PRK13947   6 LIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARLKNlVIATGGGVVLNP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  86 FNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEedlRPTLTGKPLSEEVQEVLEERDALYReVAHIIIDATN-EPSQVISEI 164
Cdd:PRK13947  86 ENVVQLRKNGVVICLKARPEVILRRVGKKKS---RPLLMVGDPEERIKELLKEREPFYD-FADYTIDTGDmTIDEVAEEI 161
PRK13946 PRK13946
shikimate kinase; Provisional
 2-170 1.42e-22

shikimate kinase; Provisional


Pssm-ID: 184411 [Multi-domain]  Cd Length: 184  Bit Score: 88.83  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   2 TQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETaaleAVTA-----PSTVIA 76
Cdd:PRK13946  10 KRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLER----RVIArllkgGPLVLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  77 TGGGIILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQaapEEDLRPTLTGKPLSEEVQEVLEERDALYREvAHIIIDATNE 156
Cdd:PRK13946  86 TGGGAFMNEETRAAIAEKGISVWLKADLDVLWERVS---RRDTRPLLRTADPKETLARLMEERYPVYAE-ADLTVASRDV 161

                        170
                 ....*....|....*
gi 446115538 157 PSQVI-SEIRSALAQ 170
Cdd:PRK13946 162 PKEVMaDEVIEALAA 176
PRK13948 PRK13948
shikimate kinase; Provisional
 7-164 9.94e-18

shikimate kinase; Provisional


Pssm-ID: 184413 [Multi-domain]  Cd Length: 182  Bit Score: 75.98  E-value: 9.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   7 LIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPS-TVIATGGGIILTE 85
Cdd:PRK13948  15 LAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLTRLDyAVISLGGGTFMHE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  86 FNRHFMQNNGIVVYLCAPVSVLVNRLQAAPeedlRPTLTGKPLSEEVQEVLEERDALYREvAHIIIDATNEPSQ-VISEI 164
Cdd:PRK13948  95 ENRRKLLSRGPVVVLWASPETIYERTRPGD----RPLLQVEDPLGRIRTLLNEREPVYRQ-ATIHVSTDGRRSEeVVEEI 169
PLN02199 PLN02199
shikimate kinase
 5-123 1.35e-16

shikimate kinase


Pssm-ID: 177850 [Multi-domain]  Cd Length: 303  Bit Score: 75.12  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMT-VAEIVEREEWAGFRARETAALEAVTAP-STVIATGGGII 82
Cdd:PLN02199 105 MYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQAMNGTsVAEIFVHHGENFFRGKETDALKKLSSRyQVVVSTGGGAV 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446115538  83 LTEFNRHFMqNNGIVVYLCAPVSVLVNRLqAAPEEDLRPTL 123
Cdd:PLN02199 185 IRPINWKYM-HKGISIWLDVPLEALAHRI-AAVGTDSRPLL 223
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
5-156 3.25e-16

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 74.94  E-value: 3.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAAL-EAVTAPSTVIATGGGIIL 83
Cdd:PRK13951   3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELLrELVERDNVVVATGGGVVI 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115538  84 TEFNRHFMQNNGiVVYLCAPVSVLVNRLqaapeedlrpTLTGKPL----SEEVQEVLEERDALYREVAHIIIDATNE 156
Cdd:PRK13951  83 DPENRELLKKEK-TLFLYAPPEVLMERV----------TTENRPLlregKERIREIWERRKQFYTEFRGIDTSKLNE 148
PRK08154 PRK08154
anaerobic benzoate catabolism transcriptional regulator; Reviewed
 7-169 1.89e-14

anaerobic benzoate catabolism transcriptional regulator; Reviewed


Pssm-ID: 236167 [Multi-domain]  Cd Length: 309  Bit Score: 69.21  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   7 LIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTA--PSTVIATGGGII-- 82
Cdd:PRK08154 138 LIGLRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVSEIFALYGQEGYRRLERRALERLIAehEEMVLATGGGIVse 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  83 -LTeFN---RHFMqnngiVVYlcapvsvlvnrLQAAPEE---------DLRPTLTGKPLSEEVQEVLEERDALYrEVAHI 149
Cdd:PRK08154 218 pAT-FDlllSHCY-----TVW-----------LKASPEEhmarvraqgDLRPMADNREAMEDLRRILASREPLY-ARADA 279

                        170       180
                 ....*....|....*....|....*
gi 446115538 150 IIDATNEP-----SQVISEIRSALA 169
Cdd:PRK08154 280 VVDTSGLTvaqslARLRELVRPALG 304
PRK00625 PRK00625
shikimate kinase; Provisional
 5-137 8.54e-14

shikimate kinase; Provisional


Pssm-ID: 134335 [Multi-domain]  Cd Length: 173  Bit Score: 65.55  E-value: 8.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQS----QLNMTVAEIVEREEWAGFRARETAALEAVTAPSTVIATGGG 80
Cdd:PRK00625   3 IFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIVSnyhgALYSSPKEIYQAYGEEGFCREEFLALTSLPVIPSIVALGGG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446115538  81 IILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAP-EEDLRPTltgKPLSEEVQEVLE 137
Cdd:PRK00625  83 TLMIEPSYAHIRNRGLLVLLSLPIATIYQRLQKRGlPERLKHA---PSLEEILSQRID 137
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 1-172 4.37e-12

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 63.34  E-value: 4.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   1 MTQPL-FLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARET-AALEAVTAPSTVIATG 78
Cdd:PRK14021   4 TRRPQaVIIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEAdVVADMLEDFDGIFSLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  79 GGIILTEFNRH----FMQNNGIVVYLCAPVSVLVNRlqaAPEEDLRPTLTGKPlSEEVQEVLEERDALYREVAHIIIDAT 154
Cdd:PRK14021  84 GGAPMTPSTQHalasYIAHGGRVVYLDADPKEAMER---ANRGGGRPMLNGDA-NKRWKKLFKQRDPVFRQVANVHVHTR 159

                        170
                 ....*....|....*....
gi 446115538 155 NEPSQVISE-IRSALAQTI 172
Cdd:PRK14021 160 GLTPQAAAKkLIDMVAERT 178
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 2-169 6.24e-06

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 43.96  E-value: 6.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   2 TQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQwLQSQLN---MTvAEI----VEREEWagFRA-RETAALEAVTAPST 73
Cdd:COG3265    1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDD-FHPPANiakMA-AGIpltdEDRAPW--LEAlADAIAAHLAAGEGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  74 VIATGGgiiLTEFNRHFMQ--NNGIV-VYLCAPVSVLVNRLQAAPEEDLRPTLtgkplseeVQ---EVLEErdaLYREVA 147
Cdd:COG3265   77 VLACSA---LKRSYRDRLRegNPDVRfVYLDGSRELIAERLAARKGHFMPASL--------LDsqfATLEP---PGPDED 142

                        170       180
                 ....*....|....*....|..
gi 446115538 148 HIIIDATNEPSQVISEIRSALA 169
Cdd:COG3265  143 AIVVDIDQPPEEIVAQILAALG 164
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 5-35 2.67e-05

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 42.24  E-value: 2.67e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQ 35
Cdd:cd02021    2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDD 32
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
12-155 7.05e-05

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 41.35  E-value: 7.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  12 GCGKTTVGMALADSLNRRFVDTDQWLQ--SQLNMTVAEIVEREEWAG-------------FRARETAALEAVTAPSTVIA 76
Cdd:COG1102   10 GSGGTTIAKRLAEKLGLPLYDGEILREaaKERGLSEEEFEKLDEKAPsllyrdtaeedeiDRALDKVIRELARKGNCVIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  77 T-GGGIILTEFNRHFMqnngivVYLCAPVSVLVNRLQAA---PEEDLRptltgkplsEEVQEVLEERDALYREVAHIII- 151
Cdd:COG1102   90 GrLADWILRDRPNVLK------VFLTAPLEVRVKRIAERegiSEEEAE---------KEIKKRDKSRAKYYKYYYGIDWg 154


                 ....
gi 446115538 152 DATN 155
Cdd:COG1102  155 DPSN 158
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 9-154 1.70e-04

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 39.78  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   9 GPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWagfRARETAALEAvtapstvIATGGGIIL----- 83
Cdd:cd02020    6 GPAGSGKSTVAKLLAKKLGLPYLDTGGIRTEEVGKLASEVAAIPEV---RKALDERQRE-------LAKKPGIVLegrdi 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  84 -TefnrHFMQNNGIVVYLCAPVSVLVNRLQaapeEDLRPTLTGKPLsEEVQEVLEERDAL--YREVA-------HIIIDA 153
Cdd:cd02020   76 gT----VVFPDADLKIFLTASPEVRAKRRA----KQLQAKGEGVDL-EEILAEIIERDERdsTRYVAplklaedAIVIDT 146


                 .
gi 446115538 154 T 154
Cdd:cd02020  147 S 147
AAA_18 pfam13238
AAA domain;
6-122 3.00e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 38.95  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538    6 FLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVE--REEWAGFRARETAALEavtaPSTVIATGGGIIL 83
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETResKRLDEDKLDRLLDLLE----ENAALEEGGNLII 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446115538   84 TEFNRHF---MQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPT 122
Cdd:pfam13238  78 DGHLAELepeRAKDLVGIVLRASPEELLERLEKRGYEEAKIK 119
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 5-31 5.47e-04

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 38.69  E-value: 5.47e-04
                         10        20
                 ....*....|....*....|....*..
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFV 31
Cdd:cd19500   40 LCLVGPPGVGKTSLGKSIARALGRKFV 66
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 5-31 1.15e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.53  E-value: 1.15e-03
                         10        20
                 ....*....|....*....|....*..
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFV 31
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFE 65
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 5-31 1.40e-03

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 36.80  E-value: 1.40e-03
                          10        20
                  ....*....|....*....|....*..
gi 446115538    5 LFLIGPRGCGKTTVGMALADSLNRRFV 31
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFI 27
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-61 2.57e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 2.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115538     3 QPLFLIGPRGCGKTTVGMALADSLNRR-----FVDTDQWLQSQLNMTVAEIVEREEWAGFRARE 61
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPgggviYIDGEDILEEVLDQLLLIIVGGKKASGSGELR 66
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 4-32 2.73e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 36.36  E-value: 2.73e-03
                         10        20
                 ....*....|....*....|....*....
gi 446115538   4 PLFLIGPRGCGKTTVGMALADSLNRRFVD 32
Cdd:cd00009   21 NLLLYGPPGTGKTTLARAIANELFRPGAP 49
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 9-31 2.76e-03

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 37.34  E-value: 2.76e-03
                         10        20
                 ....*....|....*....|...
gi 446115538   9 GPRGCGKTTVGMALADSLNRRFV 31
Cdd:COG2256   56 GPPGTGKTTLARLIANATDAEFV 78
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
5-164 3.10e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.43  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538   5 LFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEW--AGFRARETAALEAVTAPSTVIATGGGii 82
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRSDVVRKRLFGAGLAPLERSPEAtaRTYARLLALARELLAAGRSVILDATF-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538  83 LTEFNRHFM----QNNGI---VVYLCAPVSVLVNRLQA----APEEDLRPtltgkplsEEVQEVLEERDAL-YREVAHII 150
Cdd:COG0645   80 LRRAQREAFralaEEAGApfvLIWLDAPEEVLRERLEArnaeGGDSDATW--------EVLERQLAFEEPLtEDEGFLLV 151

                        170
                 ....*....|....
gi 446115538 151 IDaTNEPSQVISEI 164
Cdd:COG0645  152 VD-TSGLEEALAAL 164
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 4-88 3.36e-03

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 36.12  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115538    4 PLFLIGPRGCGKTTVGMALADSLNRRfvdtdQWLQSQLN--MTVAEIVEReewagfraRETAALEAVTAPS--TVIATGG 79
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNR-----PVFYVQLTrdTTEEDLFGR--------RNIDPGGASWVDGplVRAAREG 67

                          90
                  ....*....|
gi 446115538   80 GII-LTEFNR 88
Cdd:pfam07728  68 EIAvLDEINR 77
PBP1_NPR_B cd06384
ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B ...
 89-121 5.44e-03

ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B natriuretic peptide receptor (NPR-B). NPR-B is one of three known single membrane-spanning natriuretic peptide receptors that have been identified. Natriuretic peptides are family of structurally related but genetically distinct hormones/paracrine factors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. Like NPR-A (or GC-A), NPR-B (or GC-B) is a transmembrane guanylyl cyclase, an enzyme that catalyzes the synthesis of cGMP. NPR-B is the predominant natriuretic peptide receptor in the brain. The rank of order activation of NPR-B by natriuretic peptides is CNP>>ANP>BNP. Homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux.


Pssm-ID: 380607 [Multi-domain]  Cd Length: 399  Bit Score: 36.37  E-value: 5.44e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446115538  89 HFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRP 121
Cdd:cd06384  197 HFIKANGRIVYICGPLEMLHEIMLQAQRENLTN 229
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
4-30 9.20e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 35.69  E-value: 9.20e-03
                         10        20
                 ....*....|....*....|....*..
gi 446115538   4 PLFLIGPRGCGKTTVGMALADSLNRRF 30
Cdd:COG1373   22 AVVITGPRQVGKTTLLKQLAKELENIL 48
 
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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