NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|925193558|gb|ALC96842|]
View 

4-hydroxybutyrate CoA-transferase [Capnocytophaga sp. oral taxon 323]

Protein Classification

acetyl-CoA hydrolase/transferase family protein( domain architecture ID 11418019)

acetyl-CoA hydrolase/transferase family protein such as acetyl-CoA hydrolase, which catalyzes the hydrolysis of acetyl-CoA to form CoA and acetate, and 4-hydroxybutyrate CoA-transferase, which ferments gamma-aminobutyrate (GABA) to ammonia, acetate and butyrate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ACH1 COG0427
Propionyl CoA:succinate CoA transferase [Energy production and conversion];
3-417 0e+00

Propionyl CoA:succinate CoA transferase [Energy production and conversion];


:

Pssm-ID: 440196 [Multi-domain]  Cd Length: 427  Bit Score: 640.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558   3 KITTAQEALKVVKSGDFVYIHGGAAVPEILVDALVERAPELRNVSIGHIHIEGDAPYADPKYKDSFYVNSFFLSRNVRDI 82
Cdd:COG0427    8 KLVSAEEAASLIKSGDRVGVSTGAGEPKALPKALAARAEELFDVELVTGASLGPGALAEADLEEHFRHRSPFSGGNLRKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558  83 MKNGNGSYTPIFLSDMPLLFDRKHVKVDVVLIQVSPPDKFGFCSMGVSVEACKSAIRNAKYVIAKVNKQMPRTYGDALLH 162
Cdd:COG0427   88 INEGRVDYIPIHLSEVPRLLRSGFLPIDVALIEVSPPDEHGYFSLGTSVDNTPAAVEKAKKVIAEVNPNMPRTLGDIFIH 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 163 IDEIDFLVEHDAPIFSLHLTEPDTIEKQIARHIVPLIEDGSTLQLGIGNIPNATLGEMGHLKNLGIHTELLTEGVLDLVK 242
Cdd:COG0427  168 ISKIDAIVETDEPLPELPFAPPDEVDRAIAEHIAELIEDGATLQLGIGGIPNAVLAGLADSKDLGIHTEMLQDGMLDLIE 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 243 KGVINGYEKKIDKGKIIASFVMGTQELYDFIDKNPSVEIAEASYTNEVSVIRQNPKMISINSAIEVDLTGQVCADSIGTT 322
Cdd:COG0427  248 AGVITNASKTIDPGKIVTSFALGSKRLYDFLDDNPKVELRPVEYSNDPEVIARNLGVIAINSALEVDLYGQVNSESIGTR 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 323 IYSGFGGQIDFVRGAMLSEGGKSIIAFPSTTNKGE-SKIVPFLKQGAGVVTTRAHVQYIVTEYGVAELFGKNLCERAKAL 401
Cdd:COG0427  328 QYSGIGGQGDFARGAYLSKGGKSIIALPSTAKGGKiSRIVPMLKPGSHVTTTRHDVDYVVTEYGVADLRGKSPRERAEAL 407

                        410
                 ....*....|....*.
gi 925193558 402 IAIAHPNHRENLERSF 417
Cdd:COG0427  408 IEIAHPDFREELREYA 423
 
Name Accession Description Interval E-value
ACH1 COG0427
Propionyl CoA:succinate CoA transferase [Energy production and conversion];
3-417 0e+00

Propionyl CoA:succinate CoA transferase [Energy production and conversion];


Pssm-ID: 440196 [Multi-domain]  Cd Length: 427  Bit Score: 640.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558   3 KITTAQEALKVVKSGDFVYIHGGAAVPEILVDALVERAPELRNVSIGHIHIEGDAPYADPKYKDSFYVNSFFLSRNVRDI 82
Cdd:COG0427    8 KLVSAEEAASLIKSGDRVGVSTGAGEPKALPKALAARAEELFDVELVTGASLGPGALAEADLEEHFRHRSPFSGGNLRKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558  83 MKNGNGSYTPIFLSDMPLLFDRKHVKVDVVLIQVSPPDKFGFCSMGVSVEACKSAIRNAKYVIAKVNKQMPRTYGDALLH 162
Cdd:COG0427   88 INEGRVDYIPIHLSEVPRLLRSGFLPIDVALIEVSPPDEHGYFSLGTSVDNTPAAVEKAKKVIAEVNPNMPRTLGDIFIH 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 163 IDEIDFLVEHDAPIFSLHLTEPDTIEKQIARHIVPLIEDGSTLQLGIGNIPNATLGEMGHLKNLGIHTELLTEGVLDLVK 242
Cdd:COG0427  168 ISKIDAIVETDEPLPELPFAPPDEVDRAIAEHIAELIEDGATLQLGIGGIPNAVLAGLADSKDLGIHTEMLQDGMLDLIE 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 243 KGVINGYEKKIDKGKIIASFVMGTQELYDFIDKNPSVEIAEASYTNEVSVIRQNPKMISINSAIEVDLTGQVCADSIGTT 322
Cdd:COG0427  248 AGVITNASKTIDPGKIVTSFALGSKRLYDFLDDNPKVELRPVEYSNDPEVIARNLGVIAINSALEVDLYGQVNSESIGTR 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 323 IYSGFGGQIDFVRGAMLSEGGKSIIAFPSTTNKGE-SKIVPFLKQGAGVVTTRAHVQYIVTEYGVAELFGKNLCERAKAL 401
Cdd:COG0427  328 QYSGIGGQGDFARGAYLSKGGKSIIALPSTAKGGKiSRIVPMLKPGSHVTTTRHDVDYVVTEYGVADLRGKSPRERAEAL 407

                        410
                 ....*....|....*.
gi 925193558 402 IAIAHPNHRENLERSF 417
Cdd:COG0427  408 IEIAHPDFREELREYA 423
AcetylCoA_hyd_C pfam13336
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
 265-415 1.89e-94

Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 433126 [Multi-domain]  Cd Length: 154  Bit Score: 280.09  E-value: 1.89e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558  265 GTQELYDFIDKNPSVEIAEASYTNEVSVIRQNPKMISINSAIEVDLTGQVCADSIGTTIYSGFGGQIDFVRGAMLSEGGK 344
Cdd:pfam13336   1 GSKRLYDFLDNNPKIEMRPVDYVNDPEVIARNDKMIAINSALEVDLTGQVNSESIGGRQYSGVGGQLDFVRGAYLSKGGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925193558  345 SIIAFPSTTNKGE-SKIVPFLKQGAGVVTTRAHVQYIVTEYGVAELFGKNLCERAKALIAIAHPNHRENLER 415
Cdd:pfam13336  81 SIIALPSTAKDGTiSRIVPMLSPGAHVTTTRHDVDYVVTEYGIADLRGKSLRERAEALISIAHPDFRDELLE 152
 
Name Accession Description Interval E-value
ACH1 COG0427
Propionyl CoA:succinate CoA transferase [Energy production and conversion];
3-417 0e+00

Propionyl CoA:succinate CoA transferase [Energy production and conversion];


Pssm-ID: 440196 [Multi-domain]  Cd Length: 427  Bit Score: 640.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558   3 KITTAQEALKVVKSGDFVYIHGGAAVPEILVDALVERAPELRNVSIGHIHIEGDAPYADPKYKDSFYVNSFFLSRNVRDI 82
Cdd:COG0427    8 KLVSAEEAASLIKSGDRVGVSTGAGEPKALPKALAARAEELFDVELVTGASLGPGALAEADLEEHFRHRSPFSGGNLRKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558  83 MKNGNGSYTPIFLSDMPLLFDRKHVKVDVVLIQVSPPDKFGFCSMGVSVEACKSAIRNAKYVIAKVNKQMPRTYGDALLH 162
Cdd:COG0427   88 INEGRVDYIPIHLSEVPRLLRSGFLPIDVALIEVSPPDEHGYFSLGTSVDNTPAAVEKAKKVIAEVNPNMPRTLGDIFIH 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 163 IDEIDFLVEHDAPIFSLHLTEPDTIEKQIARHIVPLIEDGSTLQLGIGNIPNATLGEMGHLKNLGIHTELLTEGVLDLVK 242
Cdd:COG0427  168 ISKIDAIVETDEPLPELPFAPPDEVDRAIAEHIAELIEDGATLQLGIGGIPNAVLAGLADSKDLGIHTEMLQDGMLDLIE 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 243 KGVINGYEKKIDKGKIIASFVMGTQELYDFIDKNPSVEIAEASYTNEVSVIRQNPKMISINSAIEVDLTGQVCADSIGTT 322
Cdd:COG0427  248 AGVITNASKTIDPGKIVTSFALGSKRLYDFLDDNPKVELRPVEYSNDPEVIARNLGVIAINSALEVDLYGQVNSESIGTR 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558 323 IYSGFGGQIDFVRGAMLSEGGKSIIAFPSTTNKGE-SKIVPFLKQGAGVVTTRAHVQYIVTEYGVAELFGKNLCERAKAL 401
Cdd:COG0427  328 QYSGIGGQGDFARGAYLSKGGKSIIALPSTAKGGKiSRIVPMLKPGSHVTTTRHDVDYVVTEYGVADLRGKSPRERAEAL 407

                        410
                 ....*....|....*.
gi 925193558 402 IAIAHPNHRENLERSF 417
Cdd:COG0427  408 IEIAHPDFREELREYA 423
AcetylCoA_hyd_C pfam13336
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
 265-415 1.89e-94

Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 433126 [Multi-domain]  Cd Length: 154  Bit Score: 280.09  E-value: 1.89e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558  265 GTQELYDFIDKNPSVEIAEASYTNEVSVIRQNPKMISINSAIEVDLTGQVCADSIGTTIYSGFGGQIDFVRGAMLSEGGK 344
Cdd:pfam13336   1 GSKRLYDFLDNNPKIEMRPVDYVNDPEVIARNDKMIAINSALEVDLTGQVNSESIGGRQYSGVGGQLDFVRGAYLSKGGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925193558  345 SIIAFPSTTNKGE-SKIVPFLKQGAGVVTTRAHVQYIVTEYGVAELFGKNLCERAKALIAIAHPNHRENLER 415
Cdd:pfam13336  81 SIIALPSTAKDGTiSRIVPMLSPGAHVTTTRHDVDYVVTEYGIADLRGKSLRERAEALISIAHPDFRDELLE 152
AcetylCoA_hydro pfam02550
Acetyl-CoA hydrolase/transferase N-terminal domain; This family contains several enzymes which ...
 3-173 9.14e-25

Acetyl-CoA hydrolase/transferase N-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 251367  Cd Length: 198  Bit Score: 100.69  E-value: 9.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558    3 KITTAQEALKVVKSGDFVYIHG--GAAVPEILVDALVERAPELRNVSIGH-IHIE----GDAPYADPKYKDSFYVN---- 71
Cdd:pfam02550   8 KLISPEEAASLVEIGMHIERGGftFAGTAKAIPKYLAKRKVELVNAKVKTfIDLAvgafLSAGPEAEVTDWKDAFLyrpa 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925193558   72 SFFLSRNVRDIMKNGNGSYTPIFLSDMPLLFDRKHVKVDVVLIQVSPPDKFGFCSMGVSVEACKSAIRNAKYVIAKVNKQ 151
Cdd:pfam02550  88 PKQSGELGRKAINQGLASFVDKHLSEVPQLFEYGFVPIDVALIETTAMDDHGYFNFGVGCDIVKVIIEVAELVDIVMPSN 167

                         170       180
                  ....*....|....*....|...
gi 925193558  152 MPRTYG-DALLHIDEIDFLVEHD 173
Cdd:pfam02550 168 PPRRNGyDEFIAIDKVDYIVEDP 190
 
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