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Conserved domains on  [gi|359374984|gb|AEV43041|]
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acetyl-coenzyme A carboxylase, partial [Ephedrus sp. BJS-2011]

Protein Classification

biotin carboxylase domain-containing protein( domain architecture ID 1903193)

biotin carboxylase domain-containing protein similar to Blastocladiella emersonii acetyl-coenzyme-A carboxylase converts acetyl-CoA to malonyl-CoA, which is converted to malonyl-acyl carrier protein (ACP), the building block of the fatty acid moieties of bacterial membrane lipids

PubMed:  31023230

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA super family cl44129
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
2-152 9.08e-51

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG4770:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 167.88  E-value: 9.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   2 AMWALGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKG 81
Cdd:COG4770  109 AIRAMGDKIAAKKLMKAAGVPVVPGS---------------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKG 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359374984  82 IRKVDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:COG4770  168 MRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
2-152 9.08e-51

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 167.88  E-value: 9.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   2 AMWALGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKG 81
Cdd:COG4770  109 AIRAMGDKIAAKKLMKAAGVPVVPGS---------------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKG 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359374984  82 IRKVDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:COG4770  168 MRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 2-152 2.20e-45

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 153.80  E-value: 2.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   2 AMWALGDKIASSIVAQTAEVPTLPwsGSglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKG 81
Cdd:PRK08591 109 TIRLMGDKVTAKATMKKAGVPVVP--GS-------------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRG 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359374984  82 IRKVDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK08591 168 MRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEA 242
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 8-152 1.01e-34

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: 120.10  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984    8 DKIASSIVAQTAEVPTLPwsgsglkaqysgkkikiSSElfkkGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDN 87
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVP-----------------GTA----GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARN 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359374984   88 AEEIPTLFRQVQTEVPGSP----IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:pfam02786  60 EEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVA 128
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 6-154 1.46e-33

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 124.17  E-value: 1.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984     6 LGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKV 85
Cdd:TIGR01235  113 LGDKVAARNLAIKAGVPVVPGT---------------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVV 171

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359374984    86 DNAEEIPTLFRQVQTEVPGS----PIFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEALA 154
Cdd:TIGR01235  172 RSEADVADAFQRAKSEAKAAfgndEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPA 244
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
2-152 9.08e-51

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 167.88  E-value: 9.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   2 AMWALGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKG 81
Cdd:COG4770  109 AIRAMGDKIAAKKLMKAAGVPVVPGS---------------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKG 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359374984  82 IRKVDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:COG4770  168 MRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 3-152 2.28e-46

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: 161.02  E-value: 2.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984    3 MWALGDKIASSIVAQTAEVPTLPwsgsglkaqysgkkikiSSElfkkGCVSTVEECLASANKIGFPVMIKASEGGGGKGI 82
Cdd:COG1038   113 LEMLGDKVAARAAAIEAGVPVIP-----------------GTE----GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGM 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359374984   83 RKVDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:COG1038   172 RVVRSEEELEEAFESARREAKaafGDDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIA 245
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 2-152 2.20e-45

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 153.80  E-value: 2.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   2 AMWALGDKIASSIVAQTAEVPTLPwsGSglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKG 81
Cdd:PRK08591 109 TIRLMGDKVTAKATMKKAGVPVVP--GS-------------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRG 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359374984  82 IRKVDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK08591 168 MRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEA 242
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 2-152 4.21e-44

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 154.53  E-value: 4.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984    2 AMWALGDKIASSIVAQTAEVPTLPwsgsglkaqysgkkikiSSElfkkGCVSTVEECLASANKIGFPVMIKASEGGGGKG 81
Cdd:PRK12999  113 VLRLLGDKVAARNAAIKAGVPVIP-----------------GSE----GPIDDIEEALEFAEEIGYPIMLKASAGGGGRG 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359374984   82 IRKVDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK12999  172 MRIVRSEEELEEAFERAKREAKaafGNDeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIA 246
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
6-152 3.82e-38

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 134.84  E-value: 3.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   6 LGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKV 85
Cdd:PRK07178 112 MGDKTEARRAMIKAGVPVTPGS---------------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRC 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359374984  86 DNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK07178 171 NSREELEQNFPRVISEATkafGSAeVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIA 241
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 5-152 1.71e-37

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 132.84  E-value: 1.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   5 ALGDKIASSIVAQTAEVPTLPWSGSGLkaqysgkkikisselfkkgcvSTVEECLASANKIGFPVMIKASEGGGGKGIRK 84
Cdd:PRK06111 112 KMGSKIEARRAMQAAGVPVVPGITTNL---------------------EDAEEAIAIARQIGYPVMLKASAGGGGIGMQL 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359374984  85 VDNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK06111 171 VETEQELTKAFESNKKRAAnffGNGeMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEA 242
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
5-152 2.05e-36

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 130.49  E-value: 2.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   5 ALGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRK 84
Cdd:PRK08654 112 AMGSKINAKKLMKKAGVPVLPGT---------------------EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRV 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359374984  85 VDNAEEIPTLF---RQVQTEVPGSP-IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK08654 171 VYSEEELEDAIestQSIAQSAFGDStVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEA 242
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 8-152 1.01e-34

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: 120.10  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984    8 DKIASSIVAQTAEVPTLPwsgsglkaqysgkkikiSSElfkkGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDN 87
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVP-----------------GTA----GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARN 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359374984   88 AEEIPTLFRQVQTEVPGSP----IFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:pfam02786  60 EEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVA 128
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
49-152 1.37e-33

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 122.13  E-value: 1.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984  49 KGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDNAEEIPTLFRQVQTEVPGS----PIFIMKLAKCARHLEVQLL 124
Cdd:PRK05586 135 EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQIL 214

                         90       100
                 ....*....|....*....|....*...
gi 359374984 125 ADNYGNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK05586 215 GDNYGNVVHLGERDCSLQRRNQKVLEEA 242
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 6-154 1.46e-33

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 124.17  E-value: 1.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984     6 LGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKV 85
Cdd:TIGR01235  113 LGDKVAARNLAIKAGVPVVPGT---------------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVV 171

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359374984    86 DNAEEIPTLFRQVQTEVPGS----PIFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEALA 154
Cdd:TIGR01235  172 RSEADVADAFQRAKSEAKAAfgndEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPA 244
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 6-152 5.06e-33

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 121.02  E-value: 5.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   6 LGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKV 85
Cdd:PRK12833 116 MGDKARARRTARRAGVPTVPGS---------------------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVA 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359374984  86 DNAEEIPTLFRQVQTEVP---GSP-IFIMKLAKCARHLEVQLLADNYgNAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK12833 175 HDAAQLAAELPLAQREAQaafGDGgVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEA 244
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 54-152 5.82e-29

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 110.29  E-value: 5.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984  54 TVEECLASANKIGFPVMIKASEGGGGKGIRKVDNAEEIPTLF----RQVQTEVPGSPIFIMKLAKCARHLEVQLLADNYG 129
Cdd:PRK08463 140 SMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYG 219

                         90       100
                 ....*....|....*....|...
gi 359374984 130 NAISLFGRDCSIQRRHQKIIEEA 152
Cdd:PRK08463 220 NIIHLCERDCSIQRRHQKVIEIA 242
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
2-154 1.08e-28

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 109.06  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   2 AMWALGDKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkKGCVSTVEECLASANKIGFPVMIKASEGGGGKG 81
Cdd:PRK08462 111 VMALMSDKSKAKEVMKRAGVPVIPGS---------------------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRG 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359374984  82 IRKVDNAEEIPTLFRQVQTEVPGS----PIFIMKLAKCARHLEVQLLADNYGNAISLFGRDCSIQRRHQKIIEEALA 154
Cdd:PRK08462 170 MRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPA 246
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1-147 2.87e-17

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: 75.68  E-value: 2.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   1 RAMWALGDKIASSIVAQTAEVPTlPWSGsglkaqysgkkikisselfkkgCVSTVEECLASANKIGFPVMIKASEGGGGK 80
Cdd:COG0439   47 EAIRAMRDKVLMREALAAAGVPV-PGFA----------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSR 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359374984  81 GIRKVDNAEEIPTLFRQVQTEV----PGSPIFIMKLAKCaRHLEVQLLADNyGNAISlfgrdCSIQRRHQK 147
Cdd:COG0439  104 GVRVVRDEEELEAALAEARAEAkagsPNGEVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQK 167
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 40-142 1.87e-07

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: 49.23  E-value: 1.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984    40 IKISSELFKKGCVSTVEECLASANKIGFPVMIKASE--GGGGKGIrkVDNAEEIPTLFRQVQTEVPGSPIFIMKLAKCAR 117
Cdd:TIGR01369  136 KEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWK 213

                           90       100
                   ....*....|....*....|....*
gi 359374984   118 HLEVQLLADNYGNAISLfgrdCSIQ 142
Cdd:TIGR01369  214 EIEYEVMRDSNDNCITV----CNME 234
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 52-127 3.44e-07

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: 48.46  E-value: 3.44e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359374984    52 VSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDNAEEIPTLFRQVQTEVPGSPIFIMKLAKCARHLEVQLLADN 127
Cdd:TIGR01369  690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDG 765
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 52-132 8.71e-07

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: 47.18  E-value: 8.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984  52 VSTVEECLASANKIGFPVMIKASE--GGGGKGIrkVDNAEEIPTLFRQVQTEVPGSPIFIMKLAKCARHLEVQLLADNYG 129
Cdd:COG0458  135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212


                 ...
gi 359374984 130 NAI 132
Cdd:COG0458  213 NVI 215
PLN02735 PLN02735
carbamoyl-phosphate synthase
 48-132 1.39e-06

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 46.70  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   48 KKGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDNAEEiptLFRQVQTEV---PGSPIFIMKLAKCARHLEVQLL 124
Cdd:PLN02735  719 KGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDAL 795


                  ....*...
gi 359374984  125 ADNYGNAI 132
Cdd:PLN02735  796 ADSEGNVV 803
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 5-92 2.61e-06

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 45.48  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   5 ALG-DKIASSIVAQTAEVPTLPWsgsglkaqysgkkikissELFKKGCVSTVEECLAsanKIGFPVMIKASEGGGGKGIR 83
Cdd:COG1181   91 ALAmDKALTKRVLAAAGLPTPPY------------------VVLRRGELADLEAIEE---ELGLPLFVKPAREGSSVGVS 149


                 ....*....
gi 359374984  84 KVDNAEEIP 92
Cdd:COG1181  150 KVKNAEELA 158
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 5-96 7.76e-06

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 44.33  E-value: 7.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   5 ALG-DKIASSIVAQTAEVPTLPWSgsglkaqysgkkikisselfkkgCVSTVEECLASANKIGFPVMIKASEGGGGKGIR 83
Cdd:PRK01372  94 ALAmDKLRTKLVWQAAGLPTPPWI-----------------------VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVS 150

                         90
                 ....*....|...
gi 359374984  84 KVDNAEEIPTLFR 96
Cdd:PRK01372 151 KVKEEDELQAALE 163
carB PRK05294
carbamoyl-phosphate synthase large subunit;
45-90 1.83e-05

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 43.55  E-value: 1.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   45 ELFKK------------GCVSTVEECLASANKIGFPVMIKAS--EGGGGKGIrkVDNAEE 90
Cdd:PRK05294  130 ELFKEamkkiglpvprsGIAHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEE 187
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 29-132 4.35e-04

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 39.57  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984   29 SGLKAQYSGKKIKISSELFKKG---------------------CVSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDN 87
Cdd:PRK12815  105 DGILEQYGVELLGTNIEAIQKGedrerfralmkelgepvpeseIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAEN 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 359374984   88 AEEIPTLFRQVQTEVPGSPIFIMK-LAKCaRHLEVQLLADNYGNAI 132
Cdd:PRK12815  185 LEELEQLFKQGLQASPIHQCLLEEsIAGW-KEIEYEVMRDRNGNCI 229
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 47-98 1.05e-03

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 37.94  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 359374984  47 FKKGCVSTVEECLAsANKIGFPVMIKASEGGGGKGIRKVDNAEEIPTLFRQV 98
Cdd:PRK12767 130 YLPESLEDFKAALA-KGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV 180
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 52-100 1.44e-03

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 37.82  E-value: 1.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 359374984  52 VSTVEECLASANKIGFPVMIKASEGG-GGKGIRKVDNAEEIPTLFRQVQT 100
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWALLGS 170
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 54-97 1.63e-03

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 37.64  E-value: 1.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 359374984   54 TVEECLASANKIGFPVMIKASEGGGGKGIRKVDNAEEIPTLFRQ 97
Cdd:PRK12815  693 DEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAE 736
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
 20-94 1.63e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 37.58  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984  20 EVPTLPWSGSGLKA--------------QYSGKKIKISSELFKKGCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKV 85
Cdd:PRK14572 111 DTLGIPYTGSGVLAsalamdktranqifLQSGQKVAPFFELEKLKYLNSPRKTLLKLESLGFPQFLKPVEGGSSVSTYKI 190


                 ....*....
gi 359374984  86 DNAEEIPTL 94
Cdd:PRK14572 191 TNAEQLMTL 199
carB PRK05294
carbamoyl-phosphate synthase large subunit;
50-126 3.84e-03

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 36.61  E-value: 3.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359374984   50 GCVSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDNAEEIPTLFRQVQTEVPGSPIFIMKLAKCARHLEVQLLAD 126
Cdd:PRK05294  688 GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD 764
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 52-82 5.08e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 36.29  E-value: 5.08e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 359374984  52 VSTVEECLASANKIGFPVMIKASEGGGGKGI 82
Cdd:PRK14016 235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 52-91 6.32e-03

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 35.69  E-value: 6.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 359374984  52 VSTVEECLASANKIGFPVMIKASEGGGGKGIRKVDNAEEI 91
Cdd:COG0189  117 TRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDAL 156
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 45-91 6.61e-03

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: 35.80  E-value: 6.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 359374984  45 ELFKK-------GCV-STVEECLASANKIGF-PVMIKA--SEGGGGK--GIRKVDNAEEI 91
Cdd:COG0045   10 ELLAKygvpvprGIVaTTPEEAVAAAEELGGpPVVVKAqvHAGGRGKagGVKLAKSPEEA 69
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 52-96 9.14e-03

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 34.92  E-value: 9.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 359374984   52 VSTVEECLASANKIGFPVMIKASEGG-GGKGIRKVDNAEEIPTLFR 96
Cdd:pfam02222  13 AESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWE 58
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 65-102 9.65e-03

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


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 34.57  E-value: 9.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 359374984   65 IGFPVMIKASEGGGGKGIRKVDNAEEIPTLFRQVQTEV 102
Cdd:pfam13535   1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEI 38
 
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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