|
Name |
Accession |
Description |
Interval |
E-value |
| metL |
PRK09466 |
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional |
1-780 |
0e+00 |
|
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
Pssm-ID: 236530 [Multi-domain] Cd Length: 810 Bit Score: 918.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 1 MVKSVHKFGGSSLSSGERYQSVTKIIIGHTQPGDCVVVSAAGKTTDTLVSLWQsYQQQDKQAVADILLQLSNHQTALIEE 80
Cdd:PRK09466 10 MGRQLHKFGGSSLADAKCYRRVAGILAEYSQPDDLVVVSAAGKTTNQLISWLK-LSQTDRLSAHQVQQTLRRYQQDLIEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 81 LLKADAKHTALAVLAQELSDVAEQASKQ--QLQEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSG---ELL 155
Cdd:PRK09466 89 LLPAEQARSLLSRLISDLERLAALLDGGinDAQYAEVVGHGEVWSARLMAALLNQQGLPAAWLDARSFLRAERAaqpQVD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 156 HAQNKQQCSQVID--ANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIK 233
Cdd:PRK09466 169 EGLSYPLLQQLLAqhPGKRLVVTGFISRNEAGETVLLGRNGSDYSATLIGALAGVERVTIWSDVAGVYSADPRKVKDACL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 234 YNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIVK-QGKAKQKRFITTLQNVDLLLVEGLNAG 312
Cdd:PRK09466 249 LPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYQPEQGSTRIERvLASGTGARIVTSLDDVCLIELQVPASH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 313 EVahvsQLIQHSLHHFIHNGDTYLVVPAGATHQVVSYFAGRANISESNLNGCAVVAPTQDVYT---LSTLAA-------- 381
Cdd:PRK09466 329 DF----KLAQKELDQLLKRAQLRPLAVGVHPDRQLLQLAYTSEVADSALKLLDDAALPGELKLregLALVALvgagvtrn 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 382 --------EVLNQQSIHPRFIHQDTGYTLLLTDQLIESDVLSLLHEKLINKGQEVALVVAGLGNVGDEFLSQLDAQFKRL 453
Cdd:PRK09466 405 plhchrfyQQLKDQPVEFIWQSEDGLSLVAVLRQGPTESLIQGLHQSLFRAEKRIGLVLFGKGNIGSRWLELFAREQSTL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 454 SD--DYSIKLVGLIRSQHMLFNASGITLGQWKKQWQHNAVAYEQADLLSVLNELDYEHKVVVDITASEQFSQLYTDFVER 531
Cdd:PRK09466 485 SArtGFEFVLVGVVDSRRSLLNYDGLDASRALAFFDDEAVEWDEESLFLWLRAHPYDELVVLDVTASEQLALQYPDFASH 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 532 DCHLISANKYAGTAASNWYNALRQSISERNLHWRYNTSVGAGLPINFALADLQNSGDKITRIEGVFSGTLSWLCSRYDGS 611
Cdd:PRK09466 565 GFHVISANKLAGSSPSNFYRQIKDAFAKTGRHWLYNATVGAGLPINHTVRDLRNSGDSILAISGIFSGTLSWLFLQFDGS 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 612 VAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILARELGIELDLNDISLQALMPDELAQGSWDDFLVNKDKLNAFIKH 691
Cdd:PRK09466 645 VPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILAREAGYEIEPDDVRVESLVPAHLEDGSLDQFFENGDELDEQMLQ 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 692 HADAANAQDAVLRYTGLLAlEQGKvsAKVGITYAPKGDALANLTPGDNIFVINSQWYNENALVIQGPGAGKEVTAAGVHS 771
Cdd:PRK09466 725 RLEAAAEQGKVLRYVARFD-ANGK--ARVGVEAVRPDHPLANLLPCDNVFAIESRWYRDNPLVIRGPGAGREVTAGAIQS 801
|
....*....
gi 2524723447 772 DLYWLVKNL 780
Cdd:PRK09466 802 DLNRLAQLL 810
|
|
| thrA |
PRK09436 |
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
5-773 |
6.67e-164 |
|
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 494.68 E-value: 6.67e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD-CVVVSAAGKTTDTLVSLWQ--SYQQQDKQAVADILLQLSNHQTALIEEL 81
Cdd:PRK09436 3 VLKFGGTSVANAERFLRVADIIESNARQEQvAVVLSAPAKVTNHLVAMIEkaAKGDDAYPEILDAERIFHELLDGLAAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 82 LKADAKHTALAVLAQ--ELSDVAEQASkqQLQE------AALLAHGELWSARLLAAYLTQLNIQACAHDARALFsVTSGE 153
Cdd:PRK09436 83 PGFDLAQLKAKVDQEfaQLKDILHGIS--LLGEcpdsvnAAIISRGERLSIAIMAAVLEARGHDVTVIDPRELL-LADGH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 154 LLHAQ-----NKQQCSQV-IDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRK 227
Cdd:PRK09436 160 YLESTvdiaeSTRRIAASfIPADHVILMPGFTAGNEKGELVTLGRNGSDYSAAILAACLDADCCEIWTDVDGVYTADPRV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 228 VEKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIVKQGKAKQKRF--ITTLQNVDLLL 305
Cdd:PRK09436 240 VPDARLLKSLSYQEAMELSYFGAKVLHPRTIAPIAQFQIPCLIKNTFNPQAPGTLIGAESDEDSLPVkgISNLNNMAMFN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 306 VEGLN-------AGEV------AHVS-QLI-----QHSLHHFIHNGDTYLVVpagathQVVSY-FAgrANISESNLN--- 362
Cdd:PRK09436 320 VSGPGmkgmvgmASRVfaalsrAGISvVLItqsssEYSISFCVPQSDAAKAK------RALEEeFA--LELKEGLLEple 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 363 ---GCAVVAPTQD-VYTLSTLAA---EVLNQQSIHPRFIHQDTGYTLLLTdqLIESDV----LSLLHEKLINKGQEVALV 431
Cdd:PRK09436 392 veeNLAIISVVGDgMRTHPGIAAkffSALGRANINIVAIAQGSSERSISV--VIDNDDatkaLRACHQSFFLSDQVLDVF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 432 VAGLGNVGDEFLSQLDAQFKRLSD-DYSIKLVGLIRSQHMLFNASGITLGQWKKQWQHNAVAYEQADLLSVLNELDYEHK 510
Cdd:PRK09436 470 VIGVGGVGGALLEQIKRQQPWLKKkNIDLRVCGIANSRKMLLDEHGIDLDNWREELAEAGEPFDLDRLIRLVKEYHLLNP 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 511 VVVDITASEQFSQLYTDFVERDCHLISANKYAGTAASNWYNALRQSISERNLHWRYNTSVGAGLPINFALADLQNSGDKI 590
Cdd:PRK09436 550 VIVDCTSSQAVADQYADFLAAGFHVVTPNKKANTSSYAYYHQLREAARKSRRKFLYETNVGAGLPVIETLQNLLNAGDEL 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 591 TRIEGVFSGTLSWLCSRYDGSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILARELGIELDLNDISLQALMPDEL 670
Cdd:PRK09436 630 LKFEGILSGSLSFIFGKLDEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILAREAGYELELEDIEVESVLPEEF 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 671 -AQGSWDDFLVNKDKLNAFIKHHADAANAQDAVLRYTGllALEQGKvsAKVGITYAPKGDALANLTPGDNIFVINSQWYN 749
Cdd:PRK09436 710 dASGSVDEFMARLPELDAEFAARVAKARAEGKVLRYVG--QIEDGK--CRVGIAEVDANHPLYKVKGGENALAFYTRYYQ 785
|
810 820
....*....|....*....|....
gi 2524723447 750 ENALVIQGPGAGKEVTAAGVHSDL 773
Cdd:PRK09436 786 PIPLVLRGYGAGNEVTAAGVFADL 809
|
|
| AAK_AK-HSDH |
cd04257 |
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ... |
4-284 |
5.17e-94 |
|
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - homoserine dehydrogenase (HSDH). These aspartokinases are found in bacteria (E. coli AKI-HSDHI, ThrA and E. coli AKII-HSDHII, MetL) and higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation.
Pssm-ID: 239790 [Multi-domain] Cd Length: 294 Bit Score: 295.26 E-value: 5.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 4 SVHKFGGSSLSSGERYQSVTKIIIGH-TQPGDCVVVSAAGKTTDTLVSLWQSYQQQDKQAvADILLQLSNHQTALIEELL 82
Cdd:cd04257 2 KVLKFGGTSLANAERIRRVADIILNAaKQEQVAVVVSAPGKVTDLLLELAELASSGDDAY-EDILQELESKHLDLITELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 KADAKHTALAVLAQ---ELSDVAEQAS----KQQLQEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELL 155
Cdd:cd04257 81 SGDAAAELLSALGNdleELKDLLEGIYllgeLPDSIRAKVLSFGERLSARLLSALLNQQGLDAAWIDARELIVTDGGYLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 156 HAQN----KQQCSQ-VIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEK 230
Cdd:cd04257 161 AVVDielsKERIKAwFSSNGKVIVVTGFIASNPQGETTTLGRNGSDYSAAILAALLDADQVEIWTDVDGVYSADPRKVKD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2524723447 231 AIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIV 284
Cdd:cd04257 241 ARLLPSLSYQEAMELSYFGAKVLHPKTIQPVAKKNIPILIKNTFNPEAPGTLIS 294
|
|
| AAK_AK-HSDH-like |
cd04243 |
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ... |
5-284 |
9.87e-93 |
|
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.
Pssm-ID: 239776 [Multi-domain] Cd Length: 293 Bit Score: 291.77 E-value: 9.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGDCVVVSAAGKTTDTLVSLWQSYQQQDkQAVADILLQLSNHQTALIEELLKA 84
Cdd:cd04243 3 VLKFGGTSVASAERIRRVADIIKSRASSPVLVVVSALGGVTNRLVALAELAASGD-DAQAIVLQEIRERHLDLIKELLSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 85 DAKHTALAVLAQELSDVAEQASKQQL-------QEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHA 157
Cdd:cd04243 82 ESAAELLAALDSLLERLKDLLEGIRLlgelsdkTRAEVLSFGELLSSRLMSAYLQEQGLPAAWLDARELLLTDDGFLNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 158 QN----KQQCSQ-VIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAI 232
Cdd:cd04243 162 VDlklsKERLAQlLAEHGKVVVTQGFIASNEDGETTTLGRGGSDYSAALLAALLDAEEVEIWTDVDGVYTADPRKVPDAR 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2524723447 233 KYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIV 284
Cdd:cd04243 242 LLKELSYDEAMELAYFGAKVLHPRTIQPAIRKNIPIFIKNTFNPEAPGTLIS 293
|
|
| AAK_AK |
cd04234 |
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ... |
5-284 |
3.08e-69 |
|
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the N-terminal catalytic domain of aspartokinase (4-L-aspartate-4-phosphotransferase;). AK is the first enzyme in the biosynthetic pathway of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. It also catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli, three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback-inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, one is a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD is the catalytic domain of the Methylomicrobium alcaliphilum ectoine AK, the first enzyme of the ectoine biosynthetic pathway, found in this bacterium, and several other halophilic/halotolerant bacteria.
Pssm-ID: 239767 [Multi-domain] Cd Length: 227 Bit Score: 227.36 E-value: 3.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGDC-VVVSAAGKTTDTLVSLwqsyqqqdkqavadillqlsnhqtalieellk 83
Cdd:cd04234 3 VQKFGGTSVASAERIKRVADIIKAYEKGNRVvVVVSAMGGVTDLLIEL-------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 84 adakhtalavlaqelsdvaeqaskqqlqeAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHAQNKQQC 163
Cdd:cd04234 51 -----------------------------ALLLSFGERLSARLLAAALRDRGIKARSLDARQAGITTDDNHGAARIIEIS 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 164 SQVI-----DANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVC 238
Cdd:cd04234 102 YERLkellaEIGKVPVVTGFIGRNEDGEITTLGRGGSDYSAAALAAALGADEVEIWTDVDGIYTADPRIVPEARLIPEIS 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2524723447 239 REQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIV 284
Cdd:cd04234 182 YDEALELAYFGAKVLHPRAVEPARKANIPIRVKNTFNPEAPGTLIT 227
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
459-773 |
6.00e-69 |
|
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440228 [Multi-domain] Cd Length: 302 Bit Score: 229.16 E-value: 6.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 459 IKLVGLIRSQHMlfNASGITLGQWKKQWqhnavayeqaDLLSVLNELDYEhkVVVDITA-SEQFSQLYTDFVERDCHLIS 537
Cdd:COG0460 15 LRVVGVAVRDGM--KPRGIDLPRWLLTT----------DLEELIKDPEID--VVVELTGgSEPARELYLAALEAGKHVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 538 ANKYAGTAAsnwYNALRQSISERNLHWRYNTSVGAGLPINFALADLQnSGDKITRIEGVFSGTLSWLCSRYD-GSVAFSD 616
Cdd:COG0460 81 ANKALLAEH---GKELFELARKNGVDLLFEAAVGGGIPIIKTLRELL-AGDRITRIEGILNGTTNYILTKMEeEGLSFSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 617 LVLEAQKMGFTEPDPREDLSGRDMQRKLLILAREL-GIELDLNDISLQALmpdelaqgswddflvnkDKLNAfikhhADA 695
Cdd:COG0460 157 ALKEAQELGYAEADPTADVEGIDAARKLAILARLAfGTPVELEDVYVEGI-----------------TRITA-----EDI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 696 ANAQDA--VLRYTGLLALEQGKVSAKVGITYAPKGDALANLTPGDNIFVINSQWYNEnaLVIQGPGAGKEVTAAGVHSDL 773
Cdd:COG0460 215 AAAKELgyVIKLLAIAERTGGGVEARVHPTLVPADHPLASVNGVDNAVLVETDAYGE--LMFYGPGAGAEPTASAVLADL 292
|
|
| MetL1 |
COG0527 |
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ... |
1-310 |
1.86e-68 |
|
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440293 [Multi-domain] Cd Length: 407 Bit Score: 231.51 E-value: 1.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 1 MVKSVHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVslwqsyqqqdkqavadillqlsnhqtALI 78
Cdd:COG0527 1 MALIVQKFGGTSVADAERIKRVADIVKKAKEAGNrvVVVVSAMGGVTDLLI--------------------------ALA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 79 EELLKadakhtalavlaqELSDvAEQAskqqlqeaALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHAQ 158
Cdd:COG0527 55 EELLG-------------EPSP-RELD--------MLLSTGEQLSAALLAMALQELGVPAVSLDGRQAGIITDDNHGKAR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 159 -----NKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIK 233
Cdd:COG0527 113 idlieTPERIRELLEEGKVVVVAGFQGVTEDGEITTLGRGGSDTTAVALAAALKADECEIWTDVDGVYTADPRIVPDARK 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524723447 234 YNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIVKQGKAKQKRF--ITTLQNVDLLLVEGLN 310
Cdd:COG0527 193 LPEISYEEMLELAYLGAKVLHPRAVEPAMKYNIPLRVRSTFNPDAPGTLITAEDEMEGPVVkgIASDKDIALITVSGVP 271
|
|
| PLN02700 |
PLN02700 |
homoserine dehydrogenase family protein |
511-773 |
4.92e-56 |
|
homoserine dehydrogenase family protein
Pssm-ID: 215377 [Multi-domain] Cd Length: 377 Bit Score: 196.92 E-value: 4.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 511 VVVDITASEQFSQLYTDFVERDCHLISANKYAGTAASNWYnalrQSISERNLHWRYNTSVGAGLPINFALADLQNSGDKI 590
Cdd:PLN02700 112 VVVDCSASMETIGALNEAVDLGCCIVLANKKPLTSTLEDY----DKLAAHPRRIRHESTVGAGLPVIASLNRILSSGDPV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 591 TRIEGVFSGTLSWLCSRYDGSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILARELGIELDLNDISLQALMPDEL 670
Cdd:PLN02700 188 HRIVGSLSGTLGYVMSELEDGKPFSEVVKQAKSLGYTEPDPRDDLGGMDVARKALILARLLGKRINMDSIKVESLYPEEM 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 671 AQG--SWDDFLVNK-DKLNAFIKHHADAANAQDAVLRYTGLLAleqgKVSAKVGITYAPKGDALANLTPGDNIFVINSQW 747
Cdd:PLN02700 268 GPDlmSTDDFLHSGlVELDLPIEERVKEASLKGCVLRYVCVIE----GSSCQVGIRELPKDSALGRLRGSDNVVEIYSRC 343
|
250 260
....*....|....*....|....*.
gi 2524723447 748 YNENALVIQGPGAGKEVTAAGVHSDL 773
Cdd:PLN02700 344 YSEQPLVIQGAGAGNDTTAAGVLADI 369
|
|
| asp_kinases |
TIGR00657 |
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ... |
5-310 |
5.80e-53 |
|
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273201 [Multi-domain] Cd Length: 441 Bit Score: 190.26 E-value: 5.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLWQSYQQQDKQAVADIllqlsnhqtalIEELL 82
Cdd:TIGR00657 4 VQKFGGTSVGNAERIRRVAKIVLKEKKKGNqvVVVVSAMAGVTDALVELAEQASPGPSKDFLEK-----------IREKH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 KADAKHTALAVLAQELSDVAEQASKQQL---QEAALLAHGELWSARLLAAYLtqlniQACAHDARALFS-----VTSGEL 154
Cdd:TIGR00657 73 IEILERLIPQAIAEELKRLLDAELVLEEkprEMDRILSFGERLSAALLSAAL-----EELGVKAVSLLGgeagiLTDSNF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 155 LHAQNKQQCSQ-----VIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVE 229
Cdd:TIGR00657 148 GRARVIIEILTerlepLLEEGIIPVVAGFQGATEKGETTTLGRGGSDYTAALLAAALKADECEIYTDVDGIYTTDPRIVP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 230 KAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIV---KQGKAKQKRFITTLQNVDLLLV 306
Cdd:TIGR00657 228 DARRIDEISYEEMLELASFGAKVLHPRTLEPAMRAKIPIVVKSTFNPEAPGTLIVastKEMEEPIVKGLSLDRNQARVTV 307
|
....
gi 2524723447 307 EGLN 310
Cdd:TIGR00657 308 SGLG 311
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
575-773 |
3.68e-50 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 173.71 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 575 PInFALADLQNSGDKITRIEGVFSGTLSWLCSRYD-GSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILAREL-G 652
Cdd:pfam00742 1 PI-IRTLRLSLAGDRITRIEGILNGTTNYILTRMEeEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAfG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 653 IELDLNDISLQALmpdelaqgswddflvnkDKLNAFikhHADAANAQDAVLRYTGLLALEQGKVSAKVGITYAPKGDALA 732
Cdd:pfam00742 80 LDVELEDVEVEGI-----------------TRLTAE---DIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524723447 733 NLTPGDNIFVINSQWYNEnaLVIQGPGAGKEVTAAGVHSDL 773
Cdd:pfam00742 140 SVKGVDNAVVIETDRYGE--LVFYGPGAGALPTASAVLADL 178
|
|
| asp_kin_monofn |
TIGR00656 |
aspartate kinase, monofunctional class; This model describes a subclass of aspartate kinases. ... |
5-310 |
5.22e-45 |
|
aspartate kinase, monofunctional class; This model describes a subclass of aspartate kinases. These are mostly Lys-sensitive and not fused to homoserine dehydrogenase, unlike some Thr-sensitive and Met-sensitive forms. Homoserine dehydrogenase is part of Thr and Met but not Lys biosynthetic pathways. Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer. The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. The protein slr0657 from Synechocystis PCC6803 is extended by a duplication of the C-terminal region corresponding to the beta chain. Incorporation of a second copy of the C-terminal domain may be quite common in this subgroup of aspartokinases. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273200 [Multi-domain] Cd Length: 400 Bit Score: 166.79 E-value: 5.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLwqsyqqqdkqavadillqlsnhqtalieell 82
Cdd:TIGR00656 4 VQKFGGTSVGSGERIKNAARIVLKEKMKGHkvVVVVSAMGGVTDELVSL------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 kadakhtalavlAQELsdVAEQASKQQLQEaaLLAHGELWSARLLAAYLTQLNIQACAHD-ARALFsVTSGELLHAQ--- 158
Cdd:TIGR00656 53 ------------AEEA--ISDEISPRERDE--LVSHGELLSSALFSSALRELGVKAIWLDgGEAGI-RTDDNFGNAKidi 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 159 --NKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNK 236
Cdd:TIGR00656 116 iaTEERLLPLLEEGIIVVVAGFQGATEKGDTTTLGRGGSDYTAALLAAALKADRVDIYTDVPGVYTTDPRVVEAAKRIDK 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524723447 237 VCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDvQTAPTDIVkqGKAKQK---RFITTLQNVDLLLVEGLN 310
Cdd:TIGR00656 196 ISYEEALELATFGAKVLHPRTVEPAMRSKVPIEVRSSFD-PSEGTLIT--NSMENPplvKGIALRKNVTRVTVHGLG 269
|
|
| PRK09084 |
PRK09084 |
aspartate kinase III; Validated |
4-286 |
4.38e-44 |
|
aspartate kinase III; Validated
Pssm-ID: 236376 [Multi-domain] Cd Length: 448 Bit Score: 165.38 E-value: 4.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 4 SVHKFGGSSLSSGERYQSVTKIIIGHTQPGdCVVVSAAGKTTDTLVSLWQSYQQQDKQAvaDILLQLSNHQTALIEELLK 83
Cdd:PRK09084 2 VVAKFGGTSVADFDAMNRSADIVLSNPNTR-LVVLSASAGVTNLLVALAEGAEPGDERL--ALLDEIRQIQYAILDRLGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 84 ADAKHTALAVLAQELSDVAEQASkQQLQEA---ALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTS----GELLH 156
Cdd:PRK09084 79 PNVVREEIERLLENITVLAEAAS-LATSPAltdELVSHGELMSTLLFVELLRERGVQAEWFDVRKVMRTDDrfgrAEPDV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 157 AQNKQQCSQVID---ANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIK 233
Cdd:PRK09084 158 AALAELAQEQLLpllAEGVVVTQGFIGSDEKGRTTTLGRGGSDYSAALLAEALNASRVEIWTDVPGIYTTDPRIVPAAKR 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2524723447 234 YNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIVKQ 286
Cdd:PRK09084 238 IDEISFEEAAEMATFGAKVLHPATLLPAVRSNIPVFVGSSKDPEAGGTWICND 290
|
|
| AAK_AK-LysC-like |
cd04244 |
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ... |
3-284 |
4.56e-42 |
|
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive AK isoenzyme found in higher plants. The lysine-sensitive AK isoenzyme is a monofunctional protein. It is involved in the overall regulation of the aspartate pathway and can be synergistically inhibited by S-adenosylmethionine. Also included in this CD is an uncharacterized LysC-like AK found in Euryarchaeota and some bacteria. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP.
Pssm-ID: 239777 [Multi-domain] Cd Length: 298 Bit Score: 155.22 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 3 KSVHKFGGSSLSSGERYQSVTKIIiGHTQPGD--CVVVSAAGKTTDTLVSLWQSYQQQDKQAVADILLQLSN-HQTALIE 79
Cdd:cd04244 1 RLVMKFGGTSVGSAERIRHVADLV-GTYAEGHevVVVVSAMGGVTDRLLLAAEAAVSGRIAGVKDFIEILRLrHIKAAKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 80 ELLKADAKHTALAVLaqELSDVAEQASK--QQLQEAA------LLAHGELWSARLLAAYLTQLNIQACAHDARALFSVT- 150
Cdd:cd04244 80 AISDEEIAEVESIID--SLLEELEKLLYgiAYLGELTprsrdyIVSFGERLSAPIFSAALRSLGIKARALDGGEAGIITd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 151 ----SGELLHA---QNKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSA 223
Cdd:cd04244 158 dnfgNARPLPAtyeRVRKRLLPMLEDGKIPVVTGFIGATEDGAITTLGRGGSDYSATIIGAALDADEIWIWKDVDGVMTA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524723447 224 DPRKVEKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIV 284
Cdd:cd04244 238 DPRIVPEARTIPRLSYAEAMELAYFGAKVLHPRTVEPAMEKGIPVRVKNTFNPEAPGTLIT 298
|
|
| AAK_AKiii-LysC-EC |
cd04258 |
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the ... |
5-284 |
7.91e-40 |
|
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKIII. AKIII is a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In E. coli, LysC is reported to be a homodimer of 50 kD subunits.
Pssm-ID: 239791 [Multi-domain] Cd Length: 292 Bit Score: 148.67 E-value: 7.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGdCVVVSAAGKTTDTLVSLWQSYQQQDKQAVADILLQLSNHQTALIEELLKA 84
Cdd:cd04258 3 VAKFGGTSVADYAAMLRCAAIVKSDASVR-LVVVSASAGVTNLLVALADAAESGEEIESIPQLHEIRAIHFAILNRLGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 85 DAKHTALAVLAQELSDVAE-QASKQQLQEA---ALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTS----GELLH 156
Cdd:cd04258 82 EELRAKLEELLEELTQLAEgAALLGELSPAsrdELLSFGERMSSLLFSEALREQGVPAEWFDVRTVLRTDSrfgrAAPDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 157 AQNKQQCSQVID---ANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIK 233
Cdd:cd04258 162 NALAELAAKLLKpllAGTVVVTQGFIGSTEKGRTTTLGRGGSDYSAALLAEALHAEELQIWTDVAGIYTTDPRICPAARA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2524723447 234 YNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIV 284
Cdd:cd04258 242 IKEISFAEAAEMATFGAKVLHPATLLPAIRKNIPVFVGSSKDPEAGGTLIT 292
|
|
| AAK_AK-DapDC |
cd04259 |
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ... |
5-273 |
1.21e-38 |
|
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. Aspartokinase is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.
Pssm-ID: 239792 [Multi-domain] Cd Length: 295 Bit Score: 145.37 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLV------------SLWQSYQQQDKQAVADILLql 70
Cdd:cd04259 3 VLKFGGTSVSSRARWDTIAKLAQKHLNTGGqpLIVCSALSGISNKLEalidqalldehhSLFNAIQSRHLNLAEQLEV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 71 sNHQTALIEELlkadakhTALAVLAQELSDVAEQASKQQlqeAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVT 150
Cdd:cd04259 81 -DADALLANDL-------AQLQRWLTGISLLKQASPRTR---AEVLALGELMSTRLGAAYLEAQGLKVKWLDARELLTAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 151 ------SGELLHAQNKQQCS------QVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTP 218
Cdd:cd04259 150 ptlggeTMNYLSARCESEYAdallqkRLADGAQLIITQGFIARNAHGETVLLGRGGSDTSAAYFAAKLQAARCEIWTDVP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2524723447 219 GVFSADPRKVEKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSS 273
Cdd:cd04259 230 GLFTANPHEVPHARLLKRLDYDEAQEIATMGAKVLHPRCIPPARRANIPMVVRST 284
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
5-272 |
2.91e-37 |
|
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.
Pssm-ID: 395565 [Multi-domain] Cd Length: 232 Bit Score: 139.42 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPG-DCVVVSAAGKTTDTLVSLWQsyqqqdkqavadillqlsnhqtalieellk 83
Cdd:pfam00696 4 VIKLGGSSLTDKERLKRLADEIAALLEEGrKLVVVHGGGAFADGLLALLG------------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 84 adakhtalavLAQELSDVAEQASKQQLQEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHaqNKQQC 163
Cdd:pfam00696 54 ----------LSPRFARLTDAETLEVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRI--DTEAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 164 SQVIDANKINVVTGFIAASADGKTvtlGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVCREQA- 242
Cdd:pfam00696 122 EELLEAGVVPVITGFIGIDPEGEL---GRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELl 198
|
250 260 270
....*....|....*....|....*....|....
gi 2524723447 243 ----NLLARLGNPVLHAKTLSPLKNSNIKLAVRS 272
Cdd:pfam00696 199 ellaSGLATGGMKVKLPAALEAARRGGIPVVIVN 232
|
|
| PRK06635 |
PRK06635 |
aspartate kinase; Reviewed |
5-275 |
5.15e-37 |
|
aspartate kinase; Reviewed
Pssm-ID: 235843 [Multi-domain] Cd Length: 404 Bit Score: 143.72 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLwqsyqqqdkqavadillqlsnhqtalieell 82
Cdd:PRK06635 5 VQKFGGTSVGDVERIKRVAERVKAEVEAGHqvVVVVSAMGGTTDELLDL------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 kadakhtalavlAQELSDVAEQAskqqlQEAALLAHGELWSARLLAAYLTQLNIQAC-------------AH-DARALfS 148
Cdd:PRK06635 54 ------------AKEVSPLPDPR-----ELDMLLSTGEQVSVALLAMALQSLGVKARsftgwqagiitdsAHgKARIT-D 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 149 VTSGELLHAqnkqqcsqvIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKV 228
Cdd:PRK06635 116 IDPSRIREA---------LDEGDVVVVAGFQGVDEDGEITTLGRGGSDTTAVALAAALKADECEIYTDVDGVYTTDPRIV 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2524723447 229 EKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFD 275
Cdd:PRK06635 187 PKARKLDKISYEEMLELASLGAKVLHPRSVEYAKKYNVPLRVRSSFS 233
|
|
| PRK06291 |
PRK06291 |
aspartate kinase; Provisional |
5-308 |
5.71e-36 |
|
aspartate kinase; Provisional
Pssm-ID: 235773 [Multi-domain] Cd Length: 465 Bit Score: 141.99 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLWQS-YQQQDKQAVADILLQLSNHQTALIEEL 81
Cdd:PRK06291 4 VMKFGGTSVGDGERIRHVAKLVKRYRSEGNevVVVVSAMTGVTDALLEIAEQaLDVRDIAKVKDFIADLRERHYKAIEEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 82 LKADAKHTALAVLAQELSDVAEQA-------------SKqqlqeAALLAHGELWSARLLAAYLTQLNIQACAHD------ 142
Cdd:PRK06291 84 IKDPDIREEVSKTIDSRIEELEKAlvgvsylgeltprSR-----DYILSFGERLSAPILSGALRDLGIKSVALTggeagi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 143 --------ARALfsvtsgELLHAQNKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIW 214
Cdd:PRK06291 159 itdsnfgnARPL------PKTYERVKERLEPLLKEGVIPVVTGFIGETEEGIITTLGRGGSDYSAAIIGAALDADEIWIW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 215 TDTPGVFSADPRKVEKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDvQTAPTDIVKQGKAKQKRF 294
Cdd:PRK06291 233 TDVDGVMTTDPRIVPEARVIPKISYIEAMELSYFGAKVLHPRTIEPAMEKGIPVRVKNTFN-PEFPGTLITSDSESSKRV 311
|
330
....*....|....*..
gi 2524723447 295 ---ITTLQNVDLLLVEG 308
Cdd:PRK06291 312 vkaVTLIKNVALINISG 328
|
|
| AAK_AK-DapG-like |
cd04246 |
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ... |
5-275 |
2.28e-35 |
|
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional enzymes found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species, as well as, the catalytic AK domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related isoenzymes. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. The role of the AKI isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. In Corynebacterium glutamicum and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinase isoenzyme types found in Pseudomonas, C. glutamicum, and Amycolatopsis lactamdurans. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. The B. subtilis 168 AKII aspartokinase is also described as tetrameric consisting of two alpha and two beta subunits. Some archeal aspartokinases in this group lack recognizable ACT domains.
Pssm-ID: 239779 [Multi-domain] Cd Length: 239 Bit Score: 134.16 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLwqsyqqqdkqavadillqlsnhqtalieell 82
Cdd:cd04246 3 VQKFGGTSVADIERIKRVAERIKKAVKKGYqvVVVVSAMGGTTDELIGL------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 kadakhtalavlAQELSDVAEQASKqqlqeAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHAQ---- 158
Cdd:cd04246 52 ------------AKEVSPRPSPREL-----DMLLSTGEQISAALLAMALNRLGIKAISLTGWQAGILTDDHHGNARiidi 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 159 NKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVC 238
Cdd:cd04246 115 DPKRILEALEEGDVVVVAGFQGVNEDGEITTLGRGGSDTTAVALAAALKADRCEIYTDVDGVYTADPRIVPKARKLDVIS 194
|
250 260 270
....*....|....*....|....*....|....*..
gi 2524723447 239 REQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFD 275
Cdd:cd04246 195 YDEMLEMASLGAKVLHPRSVELAKKYNVPLRVRSSFS 231
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
5-323 |
6.54e-35 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 142.91 E-value: 6.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLWQSYQQQDKQAVADILLQLSNHqtaLIEEL- 81
Cdd:PRK08961 11 VLKFGGTSVSRRHRWDTIAKIVRKRLAEGGrvLVVVSALSGVSNELEAIIAAAGAGDSASRVAAIRQRHRE---LLAELg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 82 LKADAK-HTALAVLAQELSDVAEQASKQQLQEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHAQNK 160
Cdd:PRK08961 88 VDAEAVlAERLAALQRLLDGIRALTRASLRWQAEVLGQGELLSTTLGAAYLEASGLDMGWLDAREWLTALPQPNQSEWSQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 161 Q---QC---------SQVIDANKINVVT-GFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRK 227
Cdd:PRK08961 168 YlsvSCqwqsdpalrERFAAQPAQVLITqGFIARNADGGTALLGRGGSDTSAAYFAAKLGASRVEIWTDVPGMFSANPKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 228 VEKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIVKQGK-AKQKRFITTLQNVDLLLV 306
Cdd:PRK08961 248 VPDARLLTRLDYDEAQEIATTGAKVLHPRSIKPCRDAGIPMAILDTERPDLSGTSIDGDAEpVPGVKAISRKNGIVLVSM 327
|
330 340
....*....|....*....|.
gi 2524723447 307 EGLN----AGEVAHVSQLIQH 323
Cdd:PRK08961 328 ETIGmwqqVGFLADVFTLFKK 348
|
|
| AAK_AKii-LysC-BS |
cd04261 |
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ... |
5-275 |
9.13e-35 |
|
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase isoenzyme type, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In this organism and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and theronine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides.
Pssm-ID: 239794 [Multi-domain] Cd Length: 239 Bit Score: 132.65 E-value: 9.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLwqsyqqqdkqavadillqlsnhqtalieell 82
Cdd:cd04261 3 VQKFGGTSVASIERIKRVAERIKKRKKKGNqvVVVVSAMGGTTDELIEL------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 kadakhtalavlAQELSDVAEQAskqqlQEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHAQ---- 158
Cdd:cd04261 52 ------------AKEISPRPPAR-----ELDVLLSTGEQVSIALLAMALNRLGIKAISLTGWQAGILTDGHHGKARiidi 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 159 NKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVC 238
Cdd:cd04261 115 DPDRIRELLEEGDVVIVAGFQGINEDGDITTLGRGGSDTSAVALAAALGADRCEIYTDVDGVYTADPRIVPKARKLDEIS 194
|
250 260 270
....*....|....*....|....*....|....*..
gi 2524723447 239 REQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFD 275
Cdd:cd04261 195 YDEMLEMASLGAKVLHPRSVELAKKYGVPLRVLSSFS 231
|
|
| PLN02551 |
PLN02551 |
aspartokinase |
5-304 |
2.41e-32 |
|
aspartokinase
Pssm-ID: 178166 [Multi-domain] Cd Length: 521 Bit Score: 132.16 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGDCVVVSAAGKTTDTLVSLWQSYQQQDKQAVADIllqlsnHQTALIEELLKA 84
Cdd:PLN02551 55 VMKFGGSSVASAERMREVADLILSFPDERPVVVLSAMGKTTNNLLLAGEKAVSCGVTNVSEI------EELSAIRELHLR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 85 DAKHTAL-AVLAQELSDVAEQ-----ASKQQL---QEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELL 155
Cdd:PLN02551 129 TADELGVdESVVEKLLDELEQllkgiAMMKELtprTRDYLVSFGERMSTRIFAAYLNKIGVKARQYDAFDIGFITTDDFT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 156 HAQNKQQC---------SQVIDANKINVVTGFIA-ASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADP 225
Cdd:PLN02551 209 NADILEATypavakrlhGDWIDDPAVPVVTGFLGkGWKTGAITTLGRGGSDLTATTIGKALGLREIQVWKDVDGVLTCDP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 226 RKVEKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVqTAPTDIVKQGKAKQKRFITTL---QNVD 302
Cdd:PLN02551 289 RIYPNAVPVPYLTFDEAAELAYFGAQVLHPQSMRPAREGDIPVRVKNSYNP-TAPGTLITKTRDMSKAVLTSIvlkRNVT 367
|
..
gi 2524723447 303 LL 304
Cdd:PLN02551 368 ML 369
|
|
| PRK05925 |
PRK05925 |
aspartate kinase; Provisional |
1-283 |
8.91e-31 |
|
aspartate kinase; Provisional
Pssm-ID: 235646 [Multi-domain] Cd Length: 440 Bit Score: 126.08 E-value: 8.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 1 MVKSVHKFGGSSLSSGERYQSVTKIIigHTQPGDCVVVSAAGKTTDTLVSLWQSYQQQDKQAVADILlqlSNHqtaliEE 80
Cdd:PRK05925 1 MAPLVYKFGGTSLGTAESIRRVCDII--CKEKPSFVVVSAVAGVTDLLEEFCRLSKGKREALTEKIR---EKH-----EE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 81 LLKADAKHTALAVLAQELSDVAEQASKQQLQEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFsVTSGELLHAQNK 160
Cdd:PRK05925 71 IAKELGIEFSLSPWWERLEHFEDVEEISSEDQARILAIGEDISASLICAYCCTYVLPLEFLEARQVI-LTDDQYLRAVPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 161 QQCSQ------VIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKY 234
Cdd:PRK05925 150 LALMQtawhelALQEDAIYIMQGFIGANSSGKTTVLGRGGSDFSASLIAELCKAREVRIYTDVNGIYTMDPKIIKDAQLI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2524723447 235 NKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDI 283
Cdd:PRK05925 230 PELSFEEMQNLASFGAKVLHPPMLKPCVRAGIPIFVTSTFDVTKGGTWI 278
|
|
| AAK_AKiii-YclM-BS |
cd04245 |
AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the ... |
5-271 |
7.22e-30 |
|
AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in Bacilli (Bacillus subtilis YclM) and Clostridia species. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In Bacillus subtilis (BS), YclM is reported to be a single polypeptide of 50 kD. The Bacillus subtilis 168 AKIII is induced by lysine and repressed by threonine, and it is synergistically inhibited by lysine and threonine.
Pssm-ID: 239778 [Multi-domain] Cd Length: 288 Bit Score: 120.07 E-value: 7.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVtKIIIGHTQPGDCVVVSAAG-------KTTDTLVSLWQSYQQqdKQAVADILLQLSNHQTAL 77
Cdd:cd04245 3 VVKFGGSSLASAEQFQKV-KAIVKADPERKIVVVSAPGkrfkddtKVTDLLILYAEAVLA--GEDTESIFEAIVDRYAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 78 IEEL-LKADakhtALAVLAQELSDVAEQ--ASKQQLqEAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGEL 154
Cdd:cd04245 80 ADELgLPMS----ILEEIAEILENLANLdyANPDYL-LDALKARGEYLNAQLMAAYLNYQGIDARYVIPKDAGLVVTDEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 155 LHAQNK----QQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEK 230
Cdd:cd04245 155 GNAQILpesyQKIKKLRDSDEKLVIPGFYGYSKNGDIKTFSRGGSDITGAILARGFQADLYENFTDVDGIYAANPRIVAN 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2524723447 231 A-----IKYNKVcREqanlLARLGNPVLHAKTLSPLKNSNIKLAVR 271
Cdd:cd04245 235 PkpiseMTYREM-RE----LSYAGFSVFHDEALIPAIEAGIPINIK 275
|
|
| PRK09034 |
PRK09034 |
aspartate kinase; Reviewed |
5-296 |
1.99e-29 |
|
aspartate kinase; Reviewed
Pssm-ID: 236364 [Multi-domain] Cd Length: 454 Bit Score: 122.22 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGhtqpgD----CVVVSAAGK-------TTDTLVSLWQSYQQqdKQAVADILLQLSNH 73
Cdd:PRK09034 3 VVKFGGSSLASAEQFKKVLNIVKS-----DperkIVVVSAPGKrfkedtkVTDLLILYAEAVLA--GEDYEDIFEAIIAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 74 QTALIEEL-LKADAkhtaLAVLAQELSDVAEQASKQQLQ-EAALLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTS 151
Cdd:PRK09034 76 YAEIAKELgLDADI----LEKIEEILEHLANLASRNPDRlLDAFKARGEDLNAKLIAAYLNYEGIPARYVDPKEAGIIVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 152 GELLHAQ----NKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDA---QNvciWTDTPGVFSAD 224
Cdd:PRK09034 152 DEPGNAQvlpeSYDNLKKLRDRDEKLVIPGFFGVTKDGQIVTFSRGGSDITGAILARGVKAdlyEN---FTDVDGIYAAN 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524723447 225 PRKVE--KAIK---YNKVcREqanlLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTAPTDIVKQGKAKQKRFIT 296
Cdd:PRK09034 229 PRIVKnpKSIKeitYREM-RE----LSYAGFSVFHDEALIPAYRGGIPINIKNTNNPEDPGTLIVPDRDNKNKNPIT 300
|
|
| AAK_AKi-DapG-BS |
cd04260 |
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ... |
5-274 |
3.50e-27 |
|
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional class enzyme found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains.
Pssm-ID: 239793 [Multi-domain] Cd Length: 244 Bit Score: 110.94 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGK-----TTDTLVSLwqsyqqqdkqavadillqlsnhqtal 77
Cdd:cd04260 3 VQKFGGTSVSTKERREQVAKKVKQAVDEGYkpVVVVSAMGRkgdpyATDTLINL-------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 78 ieellkADAKHTALAVLAQELsdvaeqaskqqlqeaaLLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHA 157
Cdd:cd04260 57 ------VYAENSDISPRELDL----------------LMSCGEIISAVVLTSTLRAQGLKAVALTGAQAGILTDDNYSNA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 158 Q----NKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKA-- 231
Cdd:cd04260 115 KiikvNPKKILSALKEGDVVVVAGFQGVTEDGEVTTLGRGGSDTTAAALGAALNAEYVEIYTDVDGIMTADPRVVPNAri 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2524723447 232 ---IKYNKVCReqanlLARLGNPVLHAKTLSPLKNSNIKLAVRSSF 274
Cdd:cd04260 195 ldvVSYNEVFQ-----MAHQGAKVIHPRAVEIAMQANIPIRIRSTM 235
|
|
| PRK08373 |
PRK08373 |
aspartate kinase; Validated |
5-262 |
9.61e-26 |
|
aspartate kinase; Validated
Pssm-ID: 236250 [Multi-domain] Cd Length: 341 Bit Score: 109.37 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGerYQSVTKIIIGHTQPGD-CVVVSAAGKTTDTLVSLWQSYQQQDKQAVADILLQLSNHQTALIEELLK 83
Cdd:PRK08373 7 VVKFGGSSVRYD--FEEALELVKYLSEENEvVVVVSALKGVTDKLLKLAETFDKEALEEIEEIHEEFAKRLGIDLEILSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 84 AdakhtaLAVLAQELSDVAEQASKQQLqeaalLAHGELWSARLLAAYLTQLNIQACAHDARALFsVTSGELLHA------ 157
Cdd:PRK08373 85 Y------LKKLFNSRPDLPSEALRDYI-----LSFGERLSAVLFAEALENEGIKGKVVDPWEIL-EAKGSFGNAfidikk 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 158 --QNKQQCSQVIDANKINVVTGFIAaSADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKA--IK 233
Cdd:PRK08373 153 skRNVKILYELLERGRVPVVPGFIG-NLNGFRATLGRGGSDYSAVALGVLLNAKAVLIMSDVEGIYTADPKLVPSArlIP 231
|
250 260
....*....|....*....|....*....
gi 2524723447 234 YnkVCREQANLLARLGNPVLHAKTLSPLK 262
Cdd:PRK08373 232 Y--LSYDEALIAAKLGMKALHWKAIEPVK 258
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
5-275 |
1.46e-25 |
|
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.
Pssm-ID: 239033 [Multi-domain] Cd Length: 248 Bit Score: 106.37 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVslwqsyqqqdkqavadillqlsnhqtALIEELL 82
Cdd:cd02115 1 VIKFGGSSVSSEERLRNLARILVKLASEGGrvVVVHGAGPQITDELL--------------------------AHGELLG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 KADAkhtaLAVLAQELsdvaeqaskqqlqeAALLAHGELWSARLLAAYLTQLNIQACAHDAR----ALFSVTSGELLHAQ 158
Cdd:cd02115 55 YARG----LRITDRET--------------DALAAMGEGMSNLLIAAALEQHGIKAVPLDLTqagfASPNQGHVGKITKV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 159 NKQQCSQVIDANKINVVTGFIAASADGKTvTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVC 238
Cdd:cd02115 117 STDRLKSLLENGILPILSGFGGTDEKETG-TLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELT 195
|
250 260 270
....*....|....*....|....*....|....*..
gi 2524723447 239 REQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFD 275
Cdd:cd02115 196 YEEAAELAYAGAMVLKPKAADPAARAGIPVRIANTEN 232
|
|
| PRK07431 |
PRK07431 |
aspartate kinase; Provisional |
5-275 |
5.32e-25 |
|
aspartate kinase; Provisional
Pssm-ID: 236018 [Multi-domain] Cd Length: 587 Bit Score: 110.39 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLwqsyqqqdkqavadillqlsnhqtalieell 82
Cdd:PRK07431 5 VQKFGGTSVGSVERIQAVAQRIARTKEAGNdvVVVVSAMGKTTDELVKL------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 kadakhtalavlAQELSDvaeqaSKQQLQEAALLAHGELWSARLLAAYLTQLNIQA-------------CAHD-ARALfS 148
Cdd:PRK07431 54 ------------AKEISS-----NPPRREMDMLLSTGEQVSIALLSMALHELGQPAisltgaqvgivteSEHGrARIL-E 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 149 VTSGELlhaqnkqqcSQVIDANKINVVTGF--IAASADGKTVTLGRNGSDYSATLLANYCDAqNVC-IWTDTPGVFSADP 225
Cdd:PRK07431 116 IKTDRI---------QRHLDAGKVVVVAGFqgISLSSNLEITTLGRGGSDTSAVALAAALGA-DACeIYTDVPGVLTTDP 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2524723447 226 RKVEKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFD 275
Cdd:PRK07431 186 RLVPEAQLMDEISCDEMLELASLGASVLHPRAVEIARNYGVPLVVRSSWS 235
|
|
| PRK08210 |
PRK08210 |
aspartate kinase I; Reviewed |
5-395 |
5.73e-25 |
|
aspartate kinase I; Reviewed
Pssm-ID: 236188 [Multi-domain] Cd Length: 403 Bit Score: 108.02 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGDC--VVVSAAGK-----TTDTLVSLwqsyqqqdkqavadillqlsnhqtal 77
Cdd:PRK08210 5 VQKFGGTSVSTEERRKMAVNKIKKALKEGYKvvVVVSAMGRkgdpyATDTLLSL-------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 78 ieellkADAKHTALAVLAQELsdvaeqaskqqlqeaaLLAHGELWSARLLAAYLTQLNIQACA-HDARALFsVTSGELLH 156
Cdd:PRK08210 59 ------VGEEFSEISKREQDL----------------LMSCGEIISSVVFSNMLNENGIKAVAlTGGQAGI-ITDDNFTN 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 157 AQ----NKQQCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKA- 231
Cdd:PRK08210 116 AKiievNPDRILEALEEGDVVVVAGFQGVTENGDITTLGRGGSDTTAAALGVALKAEYVDIYTDVDGIMTADPRIVEDAr 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 232 ----IKYNKVCReqanlLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDVQTApTDIVKQGKAK-----QKRFITTlqnvd 302
Cdd:PRK08210 196 lldvVSYNEVFQ-----MAYQGAKVIHPRAVEIAMQANIPLRIRSTYSDSPG-TLITSLGDAKggidvEERLITG----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 303 lllveglnageVAHVSQLIQhslhhfihngdtyLVVPAGATHQVVSY--FAGRAN--ISESNLNgcavVAPTQDVYTLST 378
Cdd:PRK08210 265 -----------IAHVSNVTQ-------------IKVKAKENAYDLQQevFKALAEagISVDFIN----IFPTEVVFTVSD 316
|
410 420
....*....|....*....|.
gi 2524723447 379 ----LAAEVLNQQSIHPRFIH 395
Cdd:PRK08210 317 edseKAKEILENLGLKPSVRE 337
|
|
| PRK06392 |
PRK06392 |
homoserine dehydrogenase; Provisional |
430-673 |
3.22e-21 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 102354 [Multi-domain] Cd Length: 326 Bit Score: 95.32 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 430 LVVAGLGNVGDEFLSQLDAQFKRLSDDYSIKLVGLIRSQHMLFNASGITLGQ---WKKQWQHNAVAYEQADLLSVLNEld 506
Cdd:PRK06392 3 ISIIGLGNVGLNVLRIIKSRNDDRRNNNGISVVSVSDSKLSYYNERGLDIGKiisYKEKGRLEEIDYEKIKFDEIFEI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 507 yEHKVVVDITASEQFS----QLYTDFVERDCHLISANKyAGTAasNWYNALRQSISERNLHWRYNTSVGAGLPInFALAD 582
Cdd:PRK06392 81 -KPDVIVDVTPASKDGirekNLYINAFEHGIDVVTANK-SGLA--NHWHDIMDSASKNRRIIRYEATVAGGVPL-FSLRD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 583 LQNSGDKITRIEGVFSGTLSWLCSRYDGSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILAREL-GIELDLNDIS 661
Cdd:PRK06392 156 YSTLPSRIKNFRGIVSSTINYVIRQEANGRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLfGKDYTLRDVT 235
|
250
....*....|..
gi 2524723447 662 LQALMPDELAQG 673
Cdd:PRK06392 236 YDGIENIDRSSM 247
|
|
| PRK08841 |
PRK08841 |
aspartate kinase; Validated |
5-276 |
2.55e-19 |
|
aspartate kinase; Validated
Pssm-ID: 181563 [Multi-domain] Cd Length: 392 Bit Score: 90.96 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSGERYQSVTKIIIGHTQPGD--CVVVSAAGKTTDTLVSLwqsyqqqdkqavadillqlsnhqtalieell 82
Cdd:PRK08841 5 VQKFGGTSVGSIERIQTVAEHIIKAKNDGNqvVVVVSAMAGETNRLLGL------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 83 kadAKHTALAVLAQELsDVaeqaskqqlqeaaLLAHGELWSARLLAAYLTQLNIQACAHDARALFSVTSGELLHAQNKQ- 161
Cdd:PRK08841 54 ---AKQVDSVPTAREL-DV-------------LLSAGEQVSMALLAMTLNKLGYAARSLTGAQANIVTDNQHNDATIKHi 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 162 ---QCSQVIDANKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVC 238
Cdd:PRK08841 117 dtsTITELLEQDQIVIVAGFQGRNENGDITTLGRGGSDTTAVALAGALNADECQIFTDVDGVYTCDPRVVKNARKLDVID 196
|
250 260 270
....*....|....*....|....*....|....*...
gi 2524723447 239 REQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFDV 276
Cdd:PRK08841 197 FPSMEAMARKGAKVLHLPSVQHAWKHSVPLRVLSSFEV 234
|
|
| AspKin_pair |
TIGR02078 |
Pyrococcus aspartate kinase subunit, putative; This family consists of proteins restricted to ... |
5-266 |
8.37e-19 |
|
Pyrococcus aspartate kinase subunit, putative; This family consists of proteins restricted to and found as paralogous pairs (typically close together) in species of Pyrococcus, a hyperthermophilic archaeal genus. Members are always found close to other genes of threonine biosynthesis and appear to represent the Pyrococcal form of aspartate kinase. Alignment to aspartokinase III from E. coli shows that 300 N-terminal and 20 C-terminal amino acids are homologous, but the form in Pyrococcus lacks ~ 100 amino acids in between. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 131133 Cd Length: 327 Bit Score: 88.31 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLSSG-ERYQSVTKIIIGHTQPgdCVVVSAAGKTTDTLVSLWQSYQQQDKQAVADILLQLS-------NHQTA 76
Cdd:TIGR02078 3 VVKFGGSSVRYAfEEALELVKSLSEEKRV--IVVVSALKGITDCLIRYANTFDKSAALEIEEIYEEFAkelgvdlNILSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 77 LIEELLKadakhtalavlaqeLSDVAEQASKQQLqeaalLAHGELWSARLLAAyltqlNIQACAHDARALFsVTSGELLH 156
Cdd:TIGR02078 81 YLKELFN--------------PPDLPKEALRDYI-----LSLGERLSAVIFAE-----GINGKVVDPWDIF-FAKGDFGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 157 A--------QNKQQCSQVIDANKINVVTGFIAaSADGKTVTLGRNGSDYSATLLANYCDAQNVCIWTDTPGVFSADPRKV 228
Cdd:TIGR02078 136 AfidikkskRNAKILYEVLESGKIPVIPGFYG-NLNGYRVTLGRGGSDYSAVALGVLLNSKLVAIMSDVEGIFTADPKLV 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 2524723447 229 EKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNI 266
Cdd:TIGR02078 215 PSARLIPYLSYEEIKIAAKLGMKALQWKAADLAKEYKI 252
|
|
| PRK06270 |
PRK06270 |
homoserine dehydrogenase; Provisional |
530-781 |
1.11e-17 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 85.30 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 530 ERDCHLISANKyaGTAASNwYNALRQSISERNLHWRYNTSVGAGLP-INFALADLqnSGDKITRIEGVFSGTLSWLCSR- 607
Cdd:PRK06270 116 ERGKHVVTSNK--GPLALA-YKELKELAKKNGVRFRYEATVGGAMPiINLAKETL--AGNDIKSIKGILNGTTNYILTRm 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 608 YDGSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILARE-LGIELDLNDISLQ---ALMPDELaqgswddflvnkd 683
Cdd:PRK06270 191 EEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSiLGADLTIKDVEVEgitKITPEAI------------- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 684 klnafikhhaDAANAQDAVLRytgLLaleqGKVSAKVGITYAPKgdalanLTPGDNIFVI----NSQWYNE---NALVIQ 756
Cdd:PRK06270 258 ----------ELAAKEGYRIK---LI----GEVSREKDLSVSPR------LVPLDHPLAVsgtlNAATFETdlaGDVTVV 314
|
250 260
....*....|....*....|....*
gi 2524723447 757 GPGAGKEVTAAGVHSDLYWLVKNLK 781
Cdd:PRK06270 315 GRGAGSIETASAILSDLIAIHDRYG 339
|
|
| PRK08374 |
PRK08374 |
homoserine dehydrogenase; Provisional |
427-773 |
4.37e-15 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 169409 [Multi-domain] Cd Length: 336 Bit Score: 77.15 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 427 EVALVVAGLGNVGDEFLSQLDAQFKRLSDDY--SIKLVGLIRSQHMLFNASGITLGQWK---------KQWQHNavaYEQ 495
Cdd:PRK08374 2 EVKVSIFGFGNVGRAVAEVLAEKSRVFKERYgvELKVVSITDTSGTIWLPEDIDLREAKevkenfgklSNWGND---YEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 496 ADL--LSVLNELDYEhkVVVDITASEQFSQLYTDFVERDCHLISANKyagTAASNWYNALRQSISERNLHWRYNTSVGAG 573
Cdd:PRK08374 79 YNFspEEIVEEIDAD--IVVDVTNDKNAHEWHLEALKEGKSVVTSNK---PPIAFHYDELLDLANERNLPYLFEATVMAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 574 LPInFALADLQNSGDKITRIEGVFSGTLSWLCSRYDGSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLIlarelgi 653
Cdd:PRK08374 154 TPI-IGLLRENLLGDTVKRIEAVVNATTTFILTRMEQGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATI------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 654 eldLNDISLQALMPDELAQGSWDDFLVNKDKlnafikhhadAANAQDAVLRytgLLA-LEQGKVSakVGITYAPKGDALA 732
Cdd:PRK08374 226 ---LHWVAFPPITFEEVGIRGIKDVTEGEIE----------RAKAKGRNVR---LVAtVEEGRIS--VKPKKLPENSPLA 287
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2524723447 733 nLTPGDNIFVINSQWYNEnaLVIQGPGAGKEVTAAGVHSDL 773
Cdd:PRK08374 288 -VEGVENAAVIKTDLLGE--LVLKGPGAGGKETASGVVTDI 325
|
|
| PRK06813 |
PRK06813 |
homoserine dehydrogenase; Validated |
427-665 |
8.65e-14 |
|
homoserine dehydrogenase; Validated
Pssm-ID: 168683 [Multi-domain] Cd Length: 346 Bit Score: 73.36 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 427 EVALVVAGLGNVGDEFLSQLDAQFKRLSDDYSIKLV--GLIRSQHMLFNASGITLgqwkkqwqHNAVAYEQADLlSVLNE 504
Cdd:PRK06813 2 KIKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVvsGVLGRNVAIHNEDGLSI--------HHLLRYGGGSC-AIEKY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 505 LDY----------EHKVVVDITASEQFS-----QLYTDFVERDCHLISANKyaGTAASNWyNALRQSISERNLHWRYNTS 569
Cdd:PRK06813 73 IEHhpeeratdniSGTVLVESTVTNLKDgnpgkQYIKQAIEKKMDIVAISK--GALVTNW-REINEAAKIANVRIRYSGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 570 VGAGLPiNFALADLQNSGDKITRIEGVFSGTLSWLCSR-YDGSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILA 648
Cdd:PRK06813 150 TAAALP-TLDIGQFSLAGCHIEKIEGILNGTTNYILTKmNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLT 228
|
250
....*....|....*...
gi 2524723447 649 REL-GIELDLNDISLQAL 665
Cdd:PRK06813 229 NSLmGTENKLTDIHIKGI 246
|
|
| AAK_AK-Hom3 |
cd04247 |
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ... |
5-259 |
2.04e-11 |
|
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single aspartokinase isoenzyme type, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies show that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size.
Pssm-ID: 239780 [Multi-domain] Cd Length: 306 Bit Score: 65.92 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 5 VHKFGGSSLssGERYQSVTKIIIGH-TQPGDCVVVSAA--------GKTT-------DTLVSLWQSYQ------QQDKQA 62
Cdd:cd04247 4 VQKFGGTSV--GKFPDNIADDIVKAyLKGNKVAVVCSArstgtkaeGTTNrllqaadEALDAQEKAFHdivediRSDHLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 63 VADILLQLSNHQTALIEELLKADAKHTALAVLAQELSDVAEQASKQqlqeaaLLAHGELWSARLLAAYLTQLNIQA---- 138
Cdd:cd04247 82 AARKFIKNPELQAELEEEINKECELLRKYLEAAKILSEISPRTKDL------VISTGEKLSCRFMAAVLRDRGVDAeyvd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 139 CAHDARALFSVTS-GELLHAQNKQQCSQVIDA--NKINVVTGFIAASADGKTVTLGRNGSDYSATLLANYCDAQNVCIWT 215
Cdd:cd04247 156 LSHIVDLDFSIEAlDQTFYDELAQVLGEKITAceNRVPVVTGFFGNVPGGLLSQIGRGYTDLCAALCAVGLNADELQIWK 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2524723447 216 DTPGVFSADPRKVEKAIKYNKVCREQANLLARLGNPVLHAKTLS 259
Cdd:cd04247 236 EVDGIFTADPRKVPTARLLPSITPEEAAELTYYGSEVIHPFTME 279
|
|
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
534-781 |
4.47e-10 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 62.40 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 534 HLISANK----YAGtaasnwyNALRQSISERNLHWRYNTSVGAGLPINFALAD-LqnSGDKITRIEGVFSGTlswlcSRY 608
Cdd:PRK06349 99 HVVTANKallaVHG-------AELFAAAEEKGVDLYFEAAVAGGIPIIKALREgL--AANRITRVMGIVNGT-----TNY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 609 ------DGSVAFSDLVLEAQKMGFTEPDPREDLSGRDMQRKLLILAReL--GIELDLNDISLQ---ALMPDELAQGswdd 677
Cdd:PRK06349 165 iltkmtEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILAS-LafGTRVDFDDVYVEgisKITAEDIAYA---- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 678 flvnkDKLNAFIKHHADAanaqdavlRYTGllaleqGKVSAKVGITYAPKGDALANLtpgDNIFvinsqwyneNALVIQ- 756
Cdd:PRK06349 240 -----KELGYRIKLLGIA--------ERTE------EGIELRVHPTLIPKSHPLANV---NGVM---------NAVFVEg 288
|
250 260 270
....*....|....*....|....*....|....
gi 2524723447 757 ---------GPGAGKEVTAAGVHSDLYWLVKNLK 781
Cdd:PRK06349 289 davgetmfyGPGAGGLPTASAVVADLVDIARNLV 322
|
|
| NAD_binding_3 |
pfam03447 |
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
434-567 |
2.94e-06 |
|
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.
Pssm-ID: 281446 [Multi-domain] Cd Length: 116 Bit Score: 46.91 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 434 GLGNVGDEFLSQLDAQfkrlSDDYSIKLVGLIRSQHMLFNasgitlgqwKKQWQHNAVAYEQADLLSVLNELDyehkVVV 513
Cdd:pfam03447 1 GCGAIGSGVLEQLLRQ----QSEIPLELVAVADRDLLSKD---------PLALLPDEPLTLDLDDLIAHPDPD----VVV 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2524723447 514 DITASEQFSQLYTDFVERDCHLISANKYAGtAASNWYNALRQSISERNLHWRYN 567
Cdd:pfam03447 64 ECASSEAVAELVLDALKAGKDVVTASKGAL-ADLALYEELREAAEANGARIYVE 116
|
|
| AAK_AK-Ectoine |
cd04248 |
AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the ... |
4-275 |
1.74e-04 |
|
AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the N-terminal catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway found in Methylomicrobium alcaliphilum, Vibrio cholerae, and other various halotolerant or halophilic bacteria. Bacteria exposed to hyperosmotic stress accumulate organic solutes called 'compatible solutes' of which ectoine, a heterocyclic amino acid, is one. Apart from its osmotic function, ectoine also exhibits a protective effect on proteins, nucleic acids and membranes against a variety of stress factors. de novo synthesis of ectoine starts with the phosphorylation of L-aspartate and shares its first two enzymatic steps with the biosynthesis of amino acids of the aspartate family: aspartokinase and L-aspartate-semialdehyde dehydrogenase. The M. alcaliphilum and the V. cholerae aspartokinases are encoded on the ectABCask operon.
Pssm-ID: 239781 [Multi-domain] Cd Length: 304 Bit Score: 44.36 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 4 SVHKFGGSSLSsgeRYQSVTKIIIG---HTQPGDCVVVSAAGKTTDTLVslwqsyqQQDKQAVADILLQLSNHQ------ 74
Cdd:cd04248 2 TVEKIGGTSMS---AFGAVLDNIILkpdSDLYGRVFVVSAYSGVTNALL-------EHKKTGAPGIYQHFVDADeawrea 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 75 -TALIEELLKADAK--HTALAVL-AQELSDVAEQASKQQLQEAA-LLAHGE------LWSAR-LLA-------AYLTQLN 135
Cdd:cd04248 72 lSALKQAMLKINEAfaDIGLDVEqADAFIGARIQDARACLHDLArLCSSGYfslaehLLAAReLLAslgeahsAFNTALL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 136 IQACAHDARaLFSVT----SGELLHAQNKQQCSQVID-ANKINVVTGFiAASADGKTVTLGRNGSDYSATLLANYCDAQN 210
Cdd:cd04248 152 LQNRGVNAR-FVDLSgwrdSGDMTLDERISEAFRDIDpRDELPIVTGY-AKCAEGLMREFDRGYSEMTFSRIAVLTGASE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524723447 211 VCIWTDTpGVFSADPRKV--EKAIKYNKVCREQANLLARLGNPVLHAKTLSPLKNSNIKLAVRSSFD 275
Cdd:cd04248 230 AIIHKEF-HLSSADPKLVgeDKARPIGRTNYDVADQLANLGMEAIHPKAAKGLRQAGIPLRVKNTFE 295
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|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
196-270 |
1.52e-03 |
|
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis. Regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinases of E. coli (Ec) and Pyrococcus furiosus (Pf) are known to function as homohexamers, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Also included in this CD are the alpha and beta subunits of the Mo storage protein (MosA and MosB) characterized as an alpha4-beta4 octamer containing an ATP-dependent, polynuclear molybdenum-oxide cluster. These and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239772 [Multi-domain] Cd Length: 229 Bit Score: 40.98 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524723447 196 DYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVCREQanLLARLGNpVLHAKTLSPLKNSNIKLAV 270
Cdd:cd04239 135 DTAAALRAEEIGADVLLKATNVDGVYDADPKKNPDAKKYDRISYDE--LLKKGLK-VMDATALTLCRRNKIPIIV 206
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|
| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
178-272 |
5.45e-03 |
|
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239786 [Multi-domain] Cd Length: 221 Bit Score: 39.15 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524723447 178 FIAASADGKTVTLGrnG------SDYSATLLANYCDAQNVCIWTDTPGVFSADPRKVEKAIKYNKVCREQanLLARLGNP 251
Cdd:cd04253 96 ALEAMFTGKIVVMG--GtepgqsTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDRLSADE--LIDIVGKS 171
|
90 100
....*....|....*....|.
gi 2524723447 252 VLHAKTLSPLKNSNIKLAVRS 272
Cdd:cd04253 172 SWKAGSNEPFDPLAAKIIERS 192
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