NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1863672949|emb|CAA9211887|]
View 

Malonyl-CoA decarboxylase [uncultured Craurococcus sp.]

Protein Classification

malonyl-CoA decarboxylase( domain architecture ID 13879812)

malonyl-CoA decarboxylase (MCD) is a key intermediate in the biosynthesis of long-chain and very long-chain fatty acids, and also has a crucial role in the regulation of fatty acid oxidation through its potent inhibition of carnitine palmitoyltransferase I

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MCD pfam05292
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 173-456 1.71e-137

Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


:

Pssm-ID: 461613  Cd Length: 245  Bit Score: 395.78  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 173 GFLELRRIDWNSPAALLEKLVSYEAVHRIRTWRDLKNRLDSDRRCYAFFHPRMPEEPLIFVEVALVKGLAGSVQRLLDEK 252
Cdd:pfam05292   1 GFLELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 253 APVLDPAQADTAIFYSINNCQRGLDGISFGNFLIKRVVALLGTELKGLKAFSTLSPIPGFCRWLQERIAEGEAGMVTEEE 332
Cdd:pfam05292  81 APPIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAKESDALLSAED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 333 LSalraaapamlalpapaeggaattsapslapetpaqTLARiLARRGWQREEALAKLLEPVLTRLCATYLVQAaspRNPK 412
Cdd:pfam05292 161 RE-----------------------------------ALAA-LDDPEWHEDPELAEALREPLLRLAARYLLRA---KRDG 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1863672949 413 RARDPVEHFHLSNGARIERLNWRGDISDKGMRESAGLMVNYLYD 456
Cdd:pfam05292 202 RPLDPVARFHLGNGARLERLNWLGDTSAKGLKQSYGLMVNYLYD 245
MCD_N pfam17408
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 83-170 2.66e-26

Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


:

Pssm-ID: 465421  Cd Length: 85  Bit Score: 101.89  E-value: 2.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949  83 FDSDEAAVRAAMDRVQAAADSAErasAQARLRRALEPPRLRLLTQFTTIPDGVKFLVDLRGELLRLMDGDPLLGALESDL 162
Cdd:pfam17408   1 FGPDPERLDKAIEAYRAAPGSDA---AEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLKGNPDLRALDRDL 77


                  ....*...
gi 1863672949 163 RGLLASWF 170
Cdd:pfam17408  78 EHLLSSWF 85
 
Name Accession Description Interval E-value
MCD pfam05292
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 173-456 1.71e-137

Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 461613  Cd Length: 245  Bit Score: 395.78  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 173 GFLELRRIDWNSPAALLEKLVSYEAVHRIRTWRDLKNRLDSDRRCYAFFHPRMPEEPLIFVEVALVKGLAGSVQRLLDEK 252
Cdd:pfam05292   1 GFLELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 253 APVLDPAQADTAIFYSINNCQRGLDGISFGNFLIKRVVALLGTELKGLKAFSTLSPIPGFCRWLQERIAEGEAGMVTEEE 332
Cdd:pfam05292  81 APPIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAKESDALLSAED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 333 LSalraaapamlalpapaeggaattsapslapetpaqTLARiLARRGWQREEALAKLLEPVLTRLCATYLVQAaspRNPK 412
Cdd:pfam05292 161 RE-----------------------------------ALAA-LDDPEWHEDPELAEALREPLLRLAARYLLRA---KRDG 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1863672949 413 RARDPVEHFHLSNGARIERLNWRGDISDKGMRESAGLMVNYLYD 456
Cdd:pfam05292 202 RPLDPVARFHLGNGARLERLNWLGDTSAKGLKQSYGLMVNYLYD 245
MCD_N pfam17408
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 83-170 2.66e-26

Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 465421  Cd Length: 85  Bit Score: 101.89  E-value: 2.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949  83 FDSDEAAVRAAMDRVQAAADSAErasAQARLRRALEPPRLRLLTQFTTIPDGVKFLVDLRGELLRLMDGDPLLGALESDL 162
Cdd:pfam17408   1 FGPDPERLDKAIEAYRAAPGSDA---AEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLKGNPDLRALDRDL 77


                  ....*...
gi 1863672949 163 RGLLASWF 170
Cdd:pfam17408  78 EHLLSSWF 85
 
Name Accession Description Interval E-value
MCD pfam05292
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 173-456 1.71e-137

Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 461613  Cd Length: 245  Bit Score: 395.78  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 173 GFLELRRIDWNSPAALLEKLVSYEAVHRIRTWRDLKNRLDSDRRCYAFFHPRMPEEPLIFVEVALVKGLAGSVQRLLDEK 252
Cdd:pfam05292   1 GFLELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 253 APVLDPAQADTAIFYSINNCQRGLDGISFGNFLIKRVVALLGTELKGLKAFSTLSPIPGFCRWLQERIAEGEAGMVTEEE 332
Cdd:pfam05292  81 APPIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAKESDALLSAED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949 333 LSalraaapamlalpapaeggaattsapslapetpaqTLARiLARRGWQREEALAKLLEPVLTRLCATYLVQAaspRNPK 412
Cdd:pfam05292 161 RE-----------------------------------ALAA-LDDPEWHEDPELAEALREPLLRLAARYLLRA---KRDG 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1863672949 413 RARDPVEHFHLSNGARIERLNWRGDISDKGMRESAGLMVNYLYD 456
Cdd:pfam05292 202 RPLDPVARFHLGNGARLERLNWLGDTSAKGLKQSYGLMVNYLYD 245
MCD_N pfam17408
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 83-170 2.66e-26

Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 465421  Cd Length: 85  Bit Score: 101.89  E-value: 2.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863672949  83 FDSDEAAVRAAMDRVQAAADSAErasAQARLRRALEPPRLRLLTQFTTIPDGVKFLVDLRGELLRLMDGDPLLGALESDL 162
Cdd:pfam17408   1 FGPDPERLDKAIEAYRAAPGSDA---AEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLKGNPDLRALDRDL 77


                  ....*...
gi 1863672949 163 RGLLASWF 170
Cdd:pfam17408  78 EHLLSSWF 85
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH