|
Name |
Accession |
Description |
Interval |
E-value |
| aroK |
PRK05057 |
shikimate kinase AroK; |
1-172 |
3.79e-129 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 359.03 E-value: 3.79e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 1 MAEKRNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLAT 80
Cdd:PRK05057 1 MAEKRNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVFDVEGEEGFRDREEKVINELTEKQGIVLAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 81 GGGSVLSKENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPRDVLEDLAVSRNALYEEVADYTVRTDDQSAKV 160
Cdd:PRK05057 81 GGGSVKSRETRNRLSARGVVVYLETTIEKQLARTQRDKKRPLLQVDDPREVLEALANERNPLYEEIADVTIRTDDQSAKV 160
|
170
....*....|..
gi 515628525 161 VANQIVKMLEER 172
Cdd:PRK05057 161 VANQIIHMLESN 172
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
1-170 |
1.66e-86 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 251.26 E-value: 1.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 1 MAEKRNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLAT 80
Cdd:PRK00131 1 MLKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLARHNLVIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 81 GGGSVLSKENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPRDVLEDLAVSRNALYEEVADYTVRTDDQSAKV 160
Cdd:PRK00131 81 GGGAVLREENRALLRERGTVVYLDASFEELLRRLRRDRNRPLLQTNDPKEKLRDLYEERDPLYEEVADITVETDGRSPEE 160
|
170
....*....|
gi 515628525 161 VANQIVKMLE 170
Cdd:PRK00131 161 VVNEILEKLE 170
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
7-171 |
2.73e-81 |
|
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: 237.72 E-value: 2.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGSVL 86
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENAVIATGGGAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 87 SKENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPRDVLEDLAVSRNALYEEVADYTVRTDDQSAKVVANQIV 166
Cdd:COG0703 81 SPENRELLKEHGTVVYLDASPETLLERLRRDDNRPLLQGEDPRERLEELLAEREPLYREVADITVDTDGRSPEEVVDEIL 160
|
....*
gi 515628525 167 KMLEE 171
Cdd:COG0703 161 EALEE 165
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
13-170 |
9.16e-69 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 205.89 E-value: 9.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 13 MGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGSVLSKENRN 92
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEHGLVIATGGGAVLSEENRD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515628525 93 RLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNP-RDVLEDLAVSRNALYEEVADYTVRTDDQSAKVVANQIVKMLE 170
Cdd:pfam01202 81 LLKERGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPeEELLELLFEERDPLYEEAADIVIDTDESSPEEVATEILEALE 159
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
6-157 |
3.62e-65 |
|
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: 196.24 E-value: 3.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 6 NIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGSV 85
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKENAVIATGGGAV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515628525 86 LSKENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPrDVLEDLAVSRNALYEEVADYTVRTDDQS 157
Cdd:cd00464 81 LREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDP-ERLRELLEEREPLYREVADLTIDTDELS 151
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
4-172 |
2.46e-46 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 149.69 E-value: 2.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 4 KRNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGG 83
Cdd:PRK13946 10 KRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGPLVLATGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 84 SVLSKENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPRDVLEDLAVSRNALYEEvADYTVRTDDQSAKVVAN 163
Cdd:PRK13946 90 AFMNEETRAAIAEKGISVWLKADLDVLWERVSRRDTRPLLRTADPKETLARLMEERYPVYAE-ADLTVASRDVPKEVMAD 168
|
....*....
gi 515628525 164 QIVKMLEER 172
Cdd:PRK13946 169 EVIEALAAY 177
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
5-167 |
1.39e-37 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 127.13 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 5 RNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGS 84
Cdd:PRK13947 2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARLKNLVIATGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 85 VLSKENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPRDVLEDLAVSRNALYeEVADYTVRTDDQSAKVVANQ 164
Cdd:PRK13947 82 VLNPENVVQLRKNGVVICLKARPEVILRRVGKKKSRPLLMVGDPEERIKELLKEREPFY-DFADYTIDTGDMTIDEVAEE 160
|
...
gi 515628525 165 IVK 167
Cdd:PRK13947 161 IIK 163
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
7-169 |
4.96e-35 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 120.43 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEqGIVLATGGGSVL 86
Cdd:PRK03731 5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAALEAVTAP-STVIATGGGIIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 87 SKENRNRLSARGIVVYLETTIE---KQLARTNRDKKRPLLQTDNPRDVLEDLAVSRNALYEEVADYTVRTDDQSAKVVAn 163
Cdd:PRK03731 84 TEENRHFMRNNGIVIYLCAPVSvlaNRLEANPEEDQRPTLTGKPISEEVAEVLAEREALYREVAHHIIDATQPPSQVVS- 162
|
....*.
gi 515628525 164 QIVKML 169
Cdd:PRK03731 163 EILSAL 168
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
9-169 |
5.94e-32 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 112.96 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 9 LVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGSVLSK 88
Cdd:PRK13948 15 LAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLTRLDYAVISLGGGTFMHE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 89 ENRNRLSARGIVVYLETTIEKQLARTnRDKKRPLLQTDNPRDVLEDLAVSRNALYEEvADYTVRTDDQSAKVVANQIVKM 168
Cdd:PRK13948 95 ENRRKLLSRGPVVVLWASPETIYERT-RPGDRPLLQVEDPLGRIRTLLNEREPVYRQ-ATIHVSTDGRRSEEVVEEIVEK 172
|
.
gi 515628525 169 L 169
Cdd:PRK13948 173 L 173
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
5-154 |
4.57e-27 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 99.80 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 5 RNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGS 84
Cdd:PRK13949 2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDFFIENRFHKTVGDIFAERGEAVFRELERNMLHEVAEFEDVVISTGGGA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515628525 85 VLSKENRNRLSARGIVVYLETTIEkQLARTNRDKK--RPLLQTDNPRDVLEDLA---VSRNALYEEvADYTVRTD 154
Cdd:PRK13949 82 PCFFDNMELMNASGTTVYLKVSPE-VLFVRLRLAKqqRPLLKGKSDEELLDFIIealEKRAPFYRQ-AKIIFNAD 154
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
9-172 |
2.53e-23 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 95.31 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 9 LVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGSVLSK 88
Cdd:PRK14021 11 IIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEADVVADMLEDFDGIFSLGGGAPMTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 89 ENRNRLSAR----GIVVYLETTIEKQLARTNRDKKRPLLQTD-NPRdvLEDLAVSRNALYEEVADYTVRTDDQSAKVVAN 163
Cdd:PRK14021 91 STQHALASYiahgGRVVYLDADPKEAMERANRGGGRPMLNGDaNKR--WKKLFKQRDPVFRQVANVHVHTRGLTPQAAAK 168
|
....*....
gi 515628525 164 QIVKMLEER 172
Cdd:PRK14021 169 KLIDMVAER 177
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
7-145 |
6.86e-23 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 94.20 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGSVL 86
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELLRELVERDNVVVATGGGVVI 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515628525 87 SKENRNRLSARGiVVYLETTIEKQLARTNRDkKRPLLQT--DNPRDVLEDlavsRNALYEE 145
Cdd:PRK13951 83 DPENRELLKKEK-TLFLYAPPEVLMERVTTE-NRPLLREgkERIREIWER----RKQFYTE 137
|
|
| PRK08154 |
PRK08154 |
anaerobic benzoate catabolism transcriptional regulator; Reviewed |
2-172 |
6.44e-21 |
|
anaerobic benzoate catabolism transcriptional regulator; Reviewed
Pssm-ID: 236167 [Multi-domain] Cd Length: 309 Bit Score: 86.93 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 2 AEKRNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEEGFRKREESVINDLTEEQG-IVLAT 80
Cdd:PRK08154 131 ARRRRIALIGLRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVSEIFALYGQEGYRRLERRALERLIAEHEeMVLAT 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 81 GGGSVLSKENRNRLSARGIVVYLETTIEKQLARTNRdkkrpllQTD-----NPRDVLEDLA---VSRNALYEEvADYTVR 152
Cdd:PRK08154 211 GGGIVSEPATFDLLLSHCYTVWLKASPEEHMARVRA-------QGDlrpmaDNREAMEDLRrilASREPLYAR-ADAVVD 282
|
170 180
....*....|....*....|
gi 515628525 153 TDDQSAKVVANQIVKMLEER 172
Cdd:PRK08154 283 TSGLTVAQSLARLRELVRPA 302
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
5-127 |
1.12e-16 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 75.50 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 5 RNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEE-RTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGG 83
Cdd:PLN02199 103 RSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQaMNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGGG 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 515628525 84 SVLSKENRNRLSaRGIVVYLETTIE---KQLARTNRDkKRPLLQTDN 127
Cdd:PLN02199 183 AVIRPINWKYMH-KGISIWLDVPLEalaHRIAAVGTD-SRPLLHDES 227
|
|
| PRK00625 |
PRK00625 |
shikimate kinase; Provisional |
6-149 |
7.51e-12 |
|
shikimate kinase; Provisional
Pssm-ID: 134335 [Multi-domain] Cd Length: 173 Bit Score: 60.15 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 6 NIFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADI----AWVFDVEGEEGFRKREESVINDLTEEQGIVlATG 81
Cdd:PRK00625 2 QIFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIVSNYHGALysspKEIYQAYGEEGFCREEFLALTSLPVIPSIV-ALG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515628525 82 GGSVLSKENRNRLSARGIVVYLE---TTIEKQLartnrdKKRPLLQTDNPRDVLEDLAVSRNALYEEVADY 149
Cdd:PRK00625 81 GGTLMIEPSYAHIRNRGLLVLLSlpiATIYQRL------QKRGLPERLKHAPSLEEILSQRIDRMRSIADY 145
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
7-113 |
3.78e-07 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 47.22 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAwvfDVEGEEGFRKREESVINDLTEEqgivLATGGGSV- 85
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSDVVRKRLFGAGLA---PLERSPEATARTYARLLALARE----LLAAGRSVi 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 515628525 86 -----LSKENRNRL----SARGI---VVYLETTIEKQLAR 113
Cdd:COG0645 75 ldatfLRRAQREAFralaEEAGApfvLIWLDAPEEVLRER 114
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
7-135 |
1.44e-06 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 45.38 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADiawvfdvEGEEGFRKREESVINDLTEEQGIVLATGGGSV- 85
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEG-------RPSISYYTDATDRTYERLHELARIALRAGRPVi 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515628525 86 -----LSKENRNRL-------SARGIVVYLET---TIEKQLARTNRDKKRPllqTDNPRDVLEDL 135
Cdd:pfam13671 75 ldatnLRRDERARLlalareyGVPVRIVVFEApeeVLRERLAARARAGGDP---SDVPEEVLDRQ 136
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
7-38 |
7.35e-06 |
|
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: 43.78 E-value: 7.35e-06
10 20 30
....*....|....*....|....*....|..
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSDTV 38
Cdd:cd02021 2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDL 33
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
11-172 |
3.89e-05 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 42.12 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 11 GPMGAGKSTIGRHLASQLHMEFLDSDTVIE--ERTGADIAWV------------FDVEGEEGFRKREESVINDLTEEQGI 76
Cdd:COG1102 7 REPGSGGTTIAKRLAEKLGLPLYDGEILREaaKERGLSEEEFekldekapsllyRDTAEEDEIDRALDKVIRELARKGNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 77 VLATGGGSVLSKENRNRLSargivVYLETTIEKqlaRTNRDKKRPLLQTDNPRDVLEDLAVSRNALYEE----------V 146
Cdd:COG1102 87 VIVGRLADWILRDRPNVLK-----VFLTAPLEV---RVKRIAEREGISEEEAEKEIKKRDKSRAKYYKYyygidwgdpsN 158
|
170 180
....*....|....*....|....*.
gi 515628525 147 ADYTVRTDDQSAKVVANQIVKMLEER 172
Cdd:COG1102 159 YDLVINTSRLGIEEAVDLILAAIEAR 184
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
7-86 |
5.56e-05 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 40.87 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEErtgaDIAWVFDVEGEEGFRKREESVINDLTEEQGIVLATGGGSVL 86
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALEN----GLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGNLI 76
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
7-42 |
1.05e-04 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 38.86 E-value: 1.05e-04
10 20 30
....*....|....*....|....*....|....*....
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQL---HMEFLDSdTVIEER 42
Cdd:cd02019 2 IAITGGSGSGKSTVAKKLAEQLggrSVVVLDE-IVILEG 39
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
7-36 |
1.59e-04 |
|
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: 40.11 E-value: 1.59e-04
10 20 30
....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDSD 36
Cdd:COG3265 4 IVVMGVSGSGKSTVGQALAERLGWPFIDGD 33
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
4-33 |
3.00e-04 |
|
proteases similar to RecA; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 39.19 E-value: 3.00e-04
10 20 30
....*....|....*....|....*....|
gi 515628525 4 KRNIFLVGPMGAGKSTIGRHLASQLHMEFL 33
Cdd:cd19481 26 PKGILLYGPPGTGKTLLAKALAGELGLPLI 55
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
7-108 |
6.20e-04 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 38.23 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHM-----EFLDSDTVieeRTG--ADIAwvFDVEG-EEGFRKREEsVINDLTEEQGIVL 78
Cdd:cd02027 2 IWLTGLSGSGKSTIARALEEKLFQrgrpvYVLDGDNV---RHGlnKDLG--FSREDrEENIRRIAE-VAKLLADAGLIVI 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 515628525 79 AtgggSVLSKENRNRLSARGIV-------VYLETTIE 108
Cdd:cd02027 76 A----AFISPYREDREAARKIIgggdfleVFVDTPLE 108
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|
| RecA-like_fidgetin |
cd19523 |
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ... |
5-33 |
7.74e-04 |
|
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This 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: 410931 [Multi-domain] Cd Length: 163 Bit Score: 38.33 E-value: 7.74e-04
10 20
....*....|....*....|....*....
gi 515628525 5 RNIFLVGPMGAGKSTIGRHLASQLHMEFL 33
Cdd:cd19523 34 RSILLFGPRGTGKTLLGRCLASQLGATFL 62
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|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
7-119 |
8.19e-04 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 38.07 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQL-----HMEFLDSDTVieeRTGADIAWVFDVEGEEGFRKREESVINDLTEEQGIVLAtg 81
Cdd:pfam01583 5 IWLTGLSGAGKSTIANALERKLfeqgrSVYVLDGDNV---RHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVIT-- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 515628525 82 ggSVLSKENRNRLSARGIV-------VYLETTIEkqlARTNRDKK 119
Cdd:pfam01583 80 --AFISPYREDREQARELHeegkfieVFVDTPLE---VCEQRDPK 119
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|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
11-35 |
1.29e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 37.70 E-value: 1.29e-03
10 20
....*....|....*....|....*
gi 515628525 11 GPMGAGKSTIGRHLASQLHMEFLDS 35
Cdd:COG0283 7 GPAGSGKSTVAKALAKRLGYHYLDT 31
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
5-56 |
1.30e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 38.39 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 515628525 5 RNIFLVGPMGAGKSTIGRHLASQLHmefldsdtvieeRTGADIaWVFDVEGE 56
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLL------------RYGARI-VIFDPGGS 243
|
|
| PRK09169 |
PRK09169 |
hypothetical protein; Validated |
9-164 |
1.64e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236394 [Multi-domain] Cd Length: 2316 Bit Score: 38.16 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 9 LVGPMGAGKSTIGRHLASQLHMEFLDSDTVIEERTGADIAWVFDVEGEegFRKREESVINDlTEEQGIVLATGGGSVLSK 88
Cdd:PRK09169 2115 IEREVGPLLQALLQKLAGGLRVDKPHSVRKIAKKIGKKIARIQALRGL--SPEQAAARVRD-ALRWEVVLPAEGFGAAVE 2191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 89 ENRNRLSARGIVVYLETTIEKQLARTNRDKKRPLLQTDNPR--------DVLEDLAVSRNaLYEEVADYTV--RTDDQSA 158
Cdd:PRK09169 2192 QARQALGAKGLRVMRINNGFAAPDTTYAGLNVNLRTAAGLDfeiqfhtaDSLRTKNKTHK-LYEKLQDLEVapARERDPA 2270
|
....*.
gi 515628525 159 KVVANQ 164
Cdd:PRK09169 2271 KRLALQ 2276
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|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
7-172 |
3.54e-03 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 36.22 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQL-----HMEFLDSDTVieeRTG--ADIawvfdvegeeGFRK--REES------VINDLT 71
Cdd:COG0529 19 VWFTGLSGSGKSTLANALERRLfergrHVYLLDGDNV---RHGlnKDL----------GFSKedRDENirrigeVAKLLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 72 EEQGIVLAtgggSVLSKENRNRLSARGIV-------VYLETTIEKqLARtnRDKK-------RPLLQT----DNPrdvle 133
Cdd:COG0529 86 DAGLIVLV----AFISPYRADREEARELIgegefieVYVDTPLEV-CEA--RDPKglyakarAGEIKNftgiDDP----- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515628525 134 dlavsrnalYE--EVADYTVRTDDQSAKVVANQIVKMLEER 172
Cdd:COG0529 154 ---------YEapENPELVLDTDKESVEESVEKILAYLEER 185
|
|
| PRK06217 |
PRK06217 |
hypothetical protein; Validated |
4-120 |
4.10e-03 |
|
hypothetical protein; Validated
Pssm-ID: 168472 Cd Length: 183 Bit Score: 36.18 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628525 4 KRNIFLVGPMGAGKSTIGRHLASQLHMEFLDSDtvieertgaDIAWV-----FDV--EGEEGFRKREEsvinDLTEEQGI 76
Cdd:PRK06217 1 MMRIHITGASGSGTTTLGAALAERLDIPHLDTD---------DYFWLptdppFTTkrPPEERLRLLLE----DLRPREGW 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 515628525 77 VLAtggGSVLsKENRNRLSARGIVVYLETTIEKQLAR-TNRDKKR 120
Cdd:PRK06217 68 VLS---GSAL-GWGDPLEPLFDLVVFLTIPPELRLERlRLREFQR 108
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
11-35 |
4.57e-03 |
|
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: 35.54 E-value: 4.57e-03
10 20
....*....|....*....|....*
gi 515628525 11 GPMGAGKSTIGRHLASQLHMEFLDS 35
Cdd:cd02020 6 GPAGSGKSTVAKLLAKKLGLPYLDT 30
|
|
| Cytidylate_kin |
pfam02224 |
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ... |
7-35 |
9.33e-03 |
|
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.
Pssm-ID: 280401 [Multi-domain] Cd Length: 211 Bit Score: 35.36 E-value: 9.33e-03
10 20
....*....|....*....|....*....
gi 515628525 7 IFLVGPMGAGKSTIGRHLASQLHMEFLDS 35
Cdd:pfam02224 1 IAIDGPSGSGKSTVARILARKLGYKYLDT 29
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