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Conserved domains on  [gi|2796056025|ref|WP_372816049|]
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acetate--CoA ligase family protein [Pyrococcus kukulkanii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PatZN super family cl34077
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
2-243 2.98e-105

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


The actual alignment was detected with superfamily member COG1042:

Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 319.76  E-value: 2.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025   2 REEAVKVIEEVLKQGRTAMVEYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMKLMSPQILHKSDAKVVMLNI 81
Cdd:COG1042   470 RERARAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNL 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025  82 KNEEELKKKWEEIHENAKKYNPNAEILGVLIAPMLKPGREVIIGVTEDPQFGHAIMFGLGGIFVEILKDVTFRLVPITEK 161
Cdd:COG1042   550 RDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEA 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025 162 DARKMITEIKAYPILAGARGEEPADIDAIVDMLLKVSQLVDELKDyIKEMDLNPVFVYnkGEGAVIVDARIILKAKEEKK 241
Cdd:COG1042   630 LAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPE-ILELDINPLLVV--PEGVVAVDARIRLAPPAPPA 706


                  ..
gi 2796056025 242 PE 243
Cdd:COG1042   707 PR 708
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
2-243 2.98e-105

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 319.76  E-value: 2.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025   2 REEAVKVIEEVLKQGRTAMVEYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMKLMSPQILHKSDAKVVMLNI 81
Cdd:COG1042   470 RERARAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNL 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025  82 KNEEELKKKWEEIHENAKKYNPNAEILGVLIAPMLKPGREVIIGVTEDPQFGHAIMFGLGGIFVEILKDVTFRLVPITEK 161
Cdd:COG1042   550 RDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEA 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025 162 DARKMITEIKAYPILAGARGEEPADIDAIVDMLLKVSQLVDELKDyIKEMDLNPVFVYnkGEGAVIVDARIILKAKEEKK 241
Cdd:COG1042   630 LAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPE-ILELDINPLLVV--PEGVVAVDARIRLAPPAPPA 706


                  ..
gi 2796056025 242 PE 243
Cdd:COG1042   707 PR 708
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 11-234 9.51e-105

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 463918 [Multi-domain]  Cd Length: 221  Bit Score: 302.47  E-value: 9.51e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025  11 EVLKQGRTAMVEYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMKLMSPQILHKSDAKVVMLNIKNEEELKKK 90
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025  91 WEEIHENAKKYNPNAEILGVLIAPMLKPGREVIIGVTEDPQFGHAIMFGLGGIFVEILKDVTFRLVPITEKDARKMITEI 170
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796056025 171 KAYPILAGARGEEPADIDAIVDMLLKVSQLVDELKdYIKEMDLNPVFVYnkGEGAVIVDARIIL 234
Cdd:pfam13549 161 RAYKLLKGYRGEPPADLDALEDVLVRVSQLVIDFP-EIRELDINPLLAD--EDGVVALDARIRL 221
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
22-62 1.25e-06

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 48.55  E-value: 1.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2796056025  22 EYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEI-GYPVAMK 62
Cdd:PRK00696    5 EYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELgGGVWVVK 46
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 26-59 1.30e-04

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 43.06  E-value: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2796056025   26 KQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPV 59
Cdd:TIGR01369  132 REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
2-243 2.98e-105

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 319.76  E-value: 2.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025   2 REEAVKVIEEVLKQGRTAMVEYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMKLMSPQILHKSDAKVVMLNI 81
Cdd:COG1042   470 RERARAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNL 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025  82 KNEEELKKKWEEIHENAKKYNPNAEILGVLIAPMLKPGREVIIGVTEDPQFGHAIMFGLGGIFVEILKDVTFRLVPITEK 161
Cdd:COG1042   550 RDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEA 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025 162 DARKMITEIKAYPILAGARGEEPADIDAIVDMLLKVSQLVDELKDyIKEMDLNPVFVYnkGEGAVIVDARIILKAKEEKK 241
Cdd:COG1042   630 LAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPE-ILELDINPLLVV--PEGVVAVDARIRLAPPAPPA 706


                  ..
gi 2796056025 242 PE 243
Cdd:COG1042   707 PR 708
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 11-234 9.51e-105

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 463918 [Multi-domain]  Cd Length: 221  Bit Score: 302.47  E-value: 9.51e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025  11 EVLKQGRTAMVEYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMKLMSPQILHKSDAKVVMLNIKNEEELKKK 90
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056025  91 WEEIHENAKKYNPNAEILGVLIAPMLKPGREVIIGVTEDPQFGHAIMFGLGGIFVEILKDVTFRLVPITEKDARKMITEI 170
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796056025 171 KAYPILAGARGEEPADIDAIVDMLLKVSQLVDELKdYIKEMDLNPVFVYnkGEGAVIVDARIIL 234
Cdd:pfam13549 161 RAYKLLKGYRGEPPADLDALEDVLVRVSQLVIDFP-EIRELDINPLLAD--EDGVVALDARIRL 221
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 22-61 5.34e-08

Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439815 [Multi-domain]  Cd Length: 388  Bit Score: 52.75  E-value: 5.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2796056025  22 EYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAM 61
Cdd:COG0045     5 EYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVV 44
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
22-62 1.25e-06

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 48.55  E-value: 1.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2796056025  22 EYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEI-GYPVAMK 62
Cdd:PRK00696    5 EYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELgGGVWVVK 46
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 26-62 2.73e-06

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 47.84  E-value: 2.73e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2796056025  26 KQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:PRK14016  219 KRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVK 255
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 26-59 1.27e-05

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 45.64  E-value: 1.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2796056025  26 KQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPV 59
Cdd:COG0458   119 KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPV 152
ATP-grasp_2 pfam08442
ATP-grasp domain;
22-61 2.92e-05

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 43.79  E-value: 2.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2796056025  22 EYEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAM 61
Cdd:pfam08442   4 EYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYV 43
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 23-62 3.92e-05

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 43.71  E-value: 3.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2796056025  23 YEAKQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:COG0439    56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVK 95
carB PRK05294
carbamoyl-phosphate synthase large subunit;
26-59 4.50e-05

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 44.32  E-value: 4.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2796056025   26 KQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPV 59
Cdd:PRK05294   133 KEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPV 166
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 26-59 1.30e-04

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 43.06  E-value: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2796056025   26 KQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPV 59
Cdd:TIGR01369  132 REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
cya_phycin_syn TIGR02068
cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and ...
 26-62 1.94e-04

cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and energy, found in most Cyanobacteria. The polymer has a backbone of L-aspartic acid, with most Asp side chain carboxyl groups attached to L-arginine. The polymer is made by this enzyme, cyanophycin synthetase, and degraded by cyanophycinase. Heterologously expressed cyanophycin synthetase in E. coli produces a closely related, water-soluble polymer with some Arg replaced by Lys. It is unclear whether enzymes that produce soluble cyanophycin-like polymers in vivo in non-Cyanobacterial species should be designated as cyanophycin synthetase itself or as a related enzyme. This model makes the designation as cyanophycin synthetase. Cyanophycin synthesis is analogous to polyhydroxyalkanoic acid (PHA) biosynthesis, except that PHA polymers lack nitrogen and may be made under nitrogen-limiting conditions. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 273950 [Multi-domain]  Cd Length: 864  Bit Score: 42.46  E-value: 1.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2796056025  26 KQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:TIGR02068 218 KEILSDAGVPVPEGTVVQSAEDAWEAAQDLGYPVVIK 254
carB PRK05294
carbamoyl-phosphate synthase large subunit;
27-59 2.44e-04

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 42.01  E-value: 2.44e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2796056025   27 QVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPV 59
Cdd:PRK05294   675 KLLEKLGIPQPPNGTATSVEEALEVAEEIGYPV 707
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 25-62 3.15e-04

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 41.60  E-value: 3.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2796056025   25 AKQVLKAYGLPVPE--EKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:COG1038    122 ARAAAIEAGVPVIPgtEGPVDDLEEALAFAEEIGYPVMLK 161
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 25-62 5.47e-04

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 40.89  E-value: 5.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2796056025   25 AKQVLKAYGLPVPE--EKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:PRK12999   123 ARNAAIKAGVPVIPgsEGPIDDIEEALEFAEEIGYPIMLK 162
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 24-62 5.55e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 40.78  E-value: 5.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2796056025  24 EAKQVLKAYGLPV---PEEKLAkTLDEALKYAKEIGYPVAMK 62
Cdd:PRK06111  118 EARRAMQAAGVPVvpgITTNLE-DAEEAIAIARQIGYPVMLK 158
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 24-62 1.53e-03

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 38.82  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2796056025  24 EAKQVLKAYGLPVPE--EKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:pfam02786   4 LFKAAMKEAGVPTVPgtAGPVETEEEALAAAKEIGYPVIIK 44
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
25-62 1.74e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 39.34  E-value: 1.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2796056025  25 AKQVLKAYGLPVPE--EKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:PRK08462  121 AKEVMKRAGVPVIPgsDGALKSYEEAKKIAKEIGYPVILK 160
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 24-62 2.31e-03

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 38.63  E-value: 2.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2796056025  24 EAKQVLKAYGLP-VP-EEKLAKTLDEALKYAKEIGYPVAMK 62
Cdd:PRK08591  118 TAKATMKKAGVPvVPgSDGPVDDEEEALAIAKEIGYPVIIK 158
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 27-59 3.89e-03

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 38.44  E-value: 3.89e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2796056025   27 QVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPV 59
Cdd:TIGR01369  675 ELLDELGIPQPKWKTATSVEEAVEFASEIGYPV 707
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 26-59 8.80e-03

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 37.26  E-value: 8.80e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2796056025   26 KQVLKAYGLPVPEEKLAKTLDEALKYAKEIGYPV 59
Cdd:PRK12815   133 RALMKELGEPVPESEIVTSVEEALAFAEKIGFPI 166
 
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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