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Conserved domains on  [gi|392357769|gb|AFM73185|]
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uridylate kinase, partial [Treponema putidum]

Protein Classification

UMP kinase( domain architecture ID 10136288)

UMP kinase catalyzes the reversible phosphorylation of UMP to UDP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 1-208 1.39e-92

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: 269.89  E-value: 1.39e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   1 DNPDFVFLDKFSKAVRGWLSqdsSRKLIMVIGGGAPARDYQNAYRtvcdlcKKNISNDEADWIGIMATRLNAQLVRAVF- 79
Cdd:cd04253   13 PEKDADFIKEYANVLRKISD---GHKVAVVVGGGRLAREYISVAR------KLGASEAFLDEIGIMATRLNARLLIAALg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  80 SDLCPNPVVYDPTTVDMFGGQILVAAGWKPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKISWED 159
Cdd:cd04253   84 DAYPPVPTSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDRLSADE 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392357769 160 FIKLVGT-EWVPGKNTPFDPIASQRAQKAGIRVICAAGKDIENLENILNG 208
Cdd:cd04253  164 LIDIVGKsSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERALKG 213
 
Name Accession Description Interval E-value
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 1-208 1.39e-92

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: 269.89  E-value: 1.39e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   1 DNPDFVFLDKFSKAVRGWLSqdsSRKLIMVIGGGAPARDYQNAYRtvcdlcKKNISNDEADWIGIMATRLNAQLVRAVF- 79
Cdd:cd04253   13 PEKDADFIKEYANVLRKISD---GHKVAVVVGGGRLAREYISVAR------KLGASEAFLDEIGIMATRLNARLLIAALg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  80 SDLCPNPVVYDPTTVDMFGGQILVAAGWKPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKISWED 159
Cdd:cd04253   84 DAYPPVPTSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDRLSADE 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392357769 160 FIKLVGT-EWVPGKNTPFDPIASQRAQKAGIRVICAAGKDIENLENILNG 208
Cdd:cd04253  164 LIDIVGKsSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERALKG 213
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 1-208 8.33e-56

uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most closely related to bacterial uridylate kinases (TIGR02075), an enzyme involved in pyrimidine biosynthesis. Members are likely, but not known, to be functionally equivalent to their bacterial counterparts. However, substantial sequence differences suggest that regulatory mechanisms may be different; the bacterial form is allosterically regulated by GTP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273956 [Multi-domain]  Cd Length: 221  Bit Score: 176.73  E-value: 8.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769    1 DNPDFVFLDKFSKAVRGWLSQdssRKLIMVIGGGAPARDYQNAYRtvcdlcKKNISNDEADWIGIMATRLNAQLVRAVFS 80
Cdd:TIGR02076  12 PEIDAEFIKEFANILRKLSDE---HKVGVVVGGGKTARRYIGVAR------ELGASETFLDEIGIDATRLNAMLLIAALG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   81 DLCpNPVVydPTTV-----DMFGGQILVAAGWKPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKI 155
Cdd:TIGR02076  83 DDA-YPKV--PENFeealeAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVDGVYDKDPKKDPDAKKFDKL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392357769  156 SWEDFIKLVG-TEWVPGKNTPFDPIASQRAQKAGIRVICAAGKDIENLENILNG 208
Cdd:TIGR02076 160 TPEELVEIVGsSSVKAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKVLKG 213
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 8-194 6.49e-23

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: 92.04  E-value: 6.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769    8 LDKFSKAVRGWLSQDssRKLIMVIGGGAPARDYQNAY----RTVCDLCKKNISNDEADWIGIMATRLNAQLVRAVFSDLC 83
Cdd:pfam00696  18 LKRLADEIAALLEEG--RKLVVVHGGGAFADGLLALLglspRFARLTDAETLEVATMDALGSLGERLNAALLAAGLPAVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   84 PNPVVYDPTTVD-----------------MFGGQILVAAGWK----PGF----STDNDAVLLAERFSGNLVVNLSNIAKV 138
Cdd:pfam00696  96 LPAAQLLATEAGfiddvvtridtealeelLEAGVVPVITGFIgidpEGElgrgSSDTLAALLAEALGADKLIILTDVDGV 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392357769  139 YTDDPKKNPEAKPIDKISWEDFIKLVGTEWVPGKNTPFDPIASQRAQKAGIRVICA 194
Cdd:pfam00696 176 YTADPRKVPDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVIV 231
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 109-162 2.36e-05

Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440294 [Multi-domain]  Cd Length: 238  Bit Score: 43.85  E-value: 2.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392357769 109 PGFSTDN-----------DAVLLAERFSGnlvvnlsniakVYTDDPKKNPEAKPIDKISWEDFIK 162
Cdd:COG0528  138 PYFTTDTaaalraieigaDVLLKATKVDG-----------VYDADPKKNPDAKKYDRLTYDEVLA 191
 
Name Accession Description Interval E-value
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 1-208 1.39e-92

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: 269.89  E-value: 1.39e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   1 DNPDFVFLDKFSKAVRGWLSqdsSRKLIMVIGGGAPARDYQNAYRtvcdlcKKNISNDEADWIGIMATRLNAQLVRAVF- 79
Cdd:cd04253   13 PEKDADFIKEYANVLRKISD---GHKVAVVVGGGRLAREYISVAR------KLGASEAFLDEIGIMATRLNARLLIAALg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  80 SDLCPNPVVYDPTTVDMFGGQILVAAGWKPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKISWED 159
Cdd:cd04253   84 DAYPPVPTSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDRLSADE 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392357769 160 FIKLVGT-EWVPGKNTPFDPIASQRAQKAGIRVICAAGKDIENLENILNG 208
Cdd:cd04253  164 LIDIVGKsSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERALKG 213
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 1-208 8.33e-56

uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most closely related to bacterial uridylate kinases (TIGR02075), an enzyme involved in pyrimidine biosynthesis. Members are likely, but not known, to be functionally equivalent to their bacterial counterparts. However, substantial sequence differences suggest that regulatory mechanisms may be different; the bacterial form is allosterically regulated by GTP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273956 [Multi-domain]  Cd Length: 221  Bit Score: 176.73  E-value: 8.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769    1 DNPDFVFLDKFSKAVRGWLSQdssRKLIMVIGGGAPARDYQNAYRtvcdlcKKNISNDEADWIGIMATRLNAQLVRAVFS 80
Cdd:TIGR02076  12 PEIDAEFIKEFANILRKLSDE---HKVGVVVGGGKTARRYIGVAR------ELGASETFLDEIGIDATRLNAMLLIAALG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   81 DLCpNPVVydPTTV-----DMFGGQILVAAGWKPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKI 155
Cdd:TIGR02076  83 DDA-YPKV--PENFeealeAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVDGVYDKDPKKDPDAKKFDKL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392357769  156 SWEDFIKLVG-TEWVPGKNTPFDPIASQRAQKAGIRVICAAGKDIENLENILNG 208
Cdd:TIGR02076 160 TPEELVEIVGsSSVKAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKVLKG 213
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 4-208 1.17e-54

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: 173.88  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   4 DFVFLDKFSKAVRGWlsQDSSRKLIMVIGGGAPARDYQNAYRtvcdlckkNISNDEADWIGIMATRLNAQLVRAVFSDLC 83
Cdd:cd04239   19 DPEVLKEIAREIKEV--VDLGVEVAIVVGGGNIARGYIAAAR--------GMPRATADYIGMLATVMNALALQDALEKLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  84 PNPVVYDPTTVD--------------MFGGQILVAAGW--KPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNP 147
Cdd:cd04239   89 VKTRVMSAIPMQgvaepyirrrairhLEKGRIVIFGGGtgNPGFTTDTAAALRAEEIGADVLLKATNVDGVYDADPKKNP 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392357769 148 EAKPIDKISWEDFIKLVGtewvpgknTPFDPIASQRAQKAGIRVICAAGKDIENLENILNG 208
Cdd:cd04239  169 DAKKYDRISYDELLKKGL--------KVMDATALTLCRRNKIPIIVFNGLKPGNLLRALKG 221
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 8-194 6.49e-23

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: 92.04  E-value: 6.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769    8 LDKFSKAVRGWLSQDssRKLIMVIGGGAPARDYQNAY----RTVCDLCKKNISNDEADWIGIMATRLNAQLVRAVFSDLC 83
Cdd:pfam00696  18 LKRLADEIAALLEEG--RKLVVVHGGGAFADGLLALLglspRFARLTDAETLEVATMDALGSLGERLNAALLAAGLPAVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   84 PNPVVYDPTTVD-----------------MFGGQILVAAGWK----PGF----STDNDAVLLAERFSGNLVVNLSNIAKV 138
Cdd:pfam00696  96 LPAAQLLATEAGfiddvvtridtealeelLEAGVVPVITGFIgidpEGElgrgSSDTLAALLAEALGADKLIILTDVDGV 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392357769  139 YTDDPKKNPEAKPIDKISWEDFIKLVGTEWVPGKNTPFDPIASQRAQKAGIRVICA 194
Cdd:pfam00696 176 YTADPRKVPDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVIV 231
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 30-162 1.74e-12

uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a phosphate from ATP. It is the first step in pyrimidine biosynthesis. GTP is an allosteric activator. In a large fraction of all bacterial genomes, the gene tends to be located immediately downstream of elongation factor Ts and upstream of ribosome recycling factor. A related protein family, believed to be equivalent in function and found in the archaea and in spirochetes, is described by a separate model, TIGR02076. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213681 [Multi-domain]  Cd Length: 232  Bit Score: 64.18  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769   30 VIGGGapardyqNAYRTVcDLCKKNISNDEADWIGIMATRLNAQLVRAVF----------SDLCPNPVV--YDPTTVD-- 95
Cdd:TIGR02075  46 VIGGG-------NIFRGV-SAAELGIDRVSADYMGMLATVINGLALRDALeklglktrvlSAISMPQICesYIRRKAIkh 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392357769   96 MFGGQILVAAGW--KPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKISWEDFIK 162
Cdd:TIGR02075 118 LEKGKVVIFSGGtgNPFFTTDTAAALRAIEINADVILKGTNVDGVYTADPKKNKDAKKYDTITYNEALK 186
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 25-203 3.63e-11

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: 60.53  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  25 RKLIMVIGGGAPARDYQNAY-RTVCDLCKKNISNDEADWIGIMATRLNAQLVRAVFSDLCPNPVVYDPTTVDMF------ 97
Cdd:cd02115   30 GRVVVVHGAGPQITDELLAHgELLGYARGLRITDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFAspnqgh 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  98 -----------------GGQILVAAG-----WK-----PGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAK 150
Cdd:cd02115  110 vgkitkvstdrlkslleNGILPILSGfggtdEKetgtlGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKVPDAK 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392357769 151 PIDKISWEDFIKLVGTEWvpgknTPFDPIASQRAQKAGIRVICAAGKDIENLE 203
Cdd:cd02115  190 LLSELTYEEAAELAYAGA-----MVLKPKAADPAARAGIPVRIANTENPGALA 237
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 114-208 8.97e-11

AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.


Pssm-ID: 239775 [Multi-domain]  Cd Length: 251  Bit Score: 59.38  E-value: 8.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769 114 DND--AVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKIS--WEDFIKLVGtewvpGKNTPFDP-------IASQ 182
Cdd:cd04242  143 DNDrlSALVAGLVNADLLILLSDVDGLYDKNPRENPDAKLIPEVEeiTDEIEAMAG-----GSGSSVGTggmrtklKAAR 217

                         90       100
                 ....*....|....*....|....*.
gi 392357769 183 RAQKAGIRVICAAGKDIENLENILNG 208
Cdd:cd04242  218 IATEAGIPVVIANGRKPDVLLDILAG 243
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 30-162 3.04e-09

UMP kinase (UMPK)-Ec, 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 kinase of E. coli (Ec) 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 and chloroplast UMPKs (this CD) 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. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239787 [Multi-domain]  Cd Length: 231  Bit Score: 54.80  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  30 VIGGGapardyqNAYRTVcDLCKKNISNDEADWIGIMATRLNAQLVRA----------VFSDLCPNPVV--YDPTTVD-- 95
Cdd:cd04254   45 VVGGG-------NIFRGA-SAAEAGMDRATADYMGMLATVINALALQDaleslgvktrVMSAIPMQGVAepYIRRRAIrh 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392357769  96 MFGGQILVAAGW--KPGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKISWEDFIK 162
Cdd:cd04254  117 LEKGRVVIFAGGtgNPFFTTDTAAALRAIEINADVILKATKVDGVYDADPKKNPNAKRYDHLTYDEVLS 185
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 109-163 5.77e-06

AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA and MosB) which are related to uridine monophosphate kinase (UMPK) enzymes that catalyze the phosphorylation of UMP by ATP, yielding UDP, and playing a key role in pyrimidine nucleotide biosynthesis. The Mo storage protein from the nitrogen-fixing bacterium, Azotobacter vinelandii, is characterized as an alpha4-beta4 octamer containing a polynuclear molybdenum-oxide cluster which is ATP-dependent to bind Mo and pH-dependent to release Mo. These and related bacterial sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239788 [Multi-domain]  Cd Length: 262  Bit Score: 45.85  E-value: 5.77e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392357769 109 PGFSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKISWEDFIKL 163
Cdd:cd04255  159 PPHRTDVGAFLLAEVIGARNLIFVKDEDGLYTADPKKNKKAEFIPEISAAELLKK 213
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 109-162 2.36e-05

Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440294 [Multi-domain]  Cd Length: 238  Bit Score: 43.85  E-value: 2.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392357769 109 PGFSTDN-----------DAVLLAERFSGnlvvnlsniakVYTDDPKKNPEAKPIDKISWEDFIK 162
Cdd:COG0528  138 PYFTTDTaaalraieigaDVLLKATKVDG-----------VYDADPKKNPDAKKYDRLTYDEVLA 191
AAK_UC cd04240
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ...
 18-211 1.17e-03

AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few bacteria. Sequences in this CD are members of the Amino Acid Kinase (AAK) superfamily.


Pssm-ID: 239773 [Multi-domain]  Cd Length: 203  Bit Score: 38.50  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  18 WLSQDSSRKLIMVIGGGAPARDYQNAYRtvcdlcKKNISNDEADWIGIMATRLNAQLvravFSDLCPNPVVYDP--TTVD 95
Cdd:cd04240   18 WLKTLSGGGVVIVPGGGPFADVVRRYQE------RKGLSDAAAHWMAILAMEQYGYL----LADLEPRLVARTLaeLTDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769  96 MFGGQILV---------AAGWKPGFSTDND--AVLLAERFSGNLVVNLSNIAKVYTDDpkknpeAKPIDKISWEDfikLV 164
Cdd:cd04240   88 LERGKIAIllpyrllldTDPLPHSWEVTSDsiAAWLAKKLGAKRLVIVTDVDGIYEKD------GKLVNEIAAAE---LL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392357769 165 GTEWVpgkntpfDPIASQRAQKAGIRVICAAGKDIENLENILNGVEF 211
Cdd:cd04240  159 GETSV-------DPAFPRLLTKYGIRCYVVNGDDPERVLAALRGREG 198
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 111-209 1.85e-03

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 38.01  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392357769 111 FSTDNDAVLLAERFSGNLVVNLSNIAKVYTDDPkknPEAKPIDKISWEDFIKLVGTEWVPGKN------TPFDPIAsqRA 184
Cdd:cd04241  147 LSGDDIVVELAKALKPERVIFLTDVDGVYDKPP---PDAKLIPEIDVGSLEDILAALGSAGTDvtggmaGKIEELL--EL 221

                         90       100
                 ....*....|....*....|....*
gi 392357769 185 QKAGIRVICAAGKDIENLENILNGV 209
Cdd:cd04241  222 ARRGIEVYIFNGDKPENLYRALLGN 246
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 99-163 2.13e-03

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: 37.90  E-value: 2.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392357769  99 GQILVAAGWKpGFSTDND------------AVLLAERFSGNLVVNLSNIAKVYTDDPKKNPEAKPIDKISWEDFIKL 163
Cdd:cd04261  126 GDVVIVAGFQ-GINEDGDittlgrggsdtsAVALAAALGADRCEIYTDVDGVYTADPRIVPKARKLDEISYDEMLEM 201
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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