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Conserved domains on  [gi|1021337389|ref|WP_063349021|]
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succinate--CoA ligase subunit alpha [Streptomyces sp. MJM8645]

Protein Classification

succinate--CoA ligase subunit alpha( domain architecture ID 11481473)

ADP-forming/GDP-forming succinate--CoA ligase subunit alpha is the coenzyme A and phosphate binding subunit of the succinyl-CoA synthetase that couples the hydrolysis of succinyl-CoA to the synthesis of ATP/GTP, as part of the citric acid cycle (TCA)

CATH:  3.40.50.261
EC:  6.2.1.-
Gene Ontology:  GO:0000166|GO:0016874|GO:0003824
SCOP:  4000071

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05678 PRK05678
succinyl-CoA synthetase subunit alpha; Validated
 1-294 0e+00

succinyl-CoA synthetase subunit alpha; Validated


:

Pssm-ID: 180194 [Multi-domain]  Cd Length: 291  Bit Score: 523.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   1 MAIFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPK 80
Cdd:PRK05678    1 MSILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVL----GLPVFNTVAEAVEATGANASVIYVPPP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  81 FTKDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKS 160
Cdd:PRK05678   77 FAADAILEAIDAGIDLIVCITEGIPVLDMLEVKAYL--ERKKTRLIGPNCPGIITPGECKIGIMPGHIHKKGRVGVVSRS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 161 GTLTYQLMYELRDIGF--SSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVTKPVVGYV 238
Cdd:PRK05678  155 GTLTYEAVAQLTDLGFgqSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKANVTKPVVGYI 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021337389 239 AGFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREIIAG 294
Cdd:PRK05678  235 AGVTAPPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKG 290
 
Name Accession Description Interval E-value
PRK05678 PRK05678
succinyl-CoA synthetase subunit alpha; Validated
 1-294 0e+00

succinyl-CoA synthetase subunit alpha; Validated


Pssm-ID: 180194 [Multi-domain]  Cd Length: 291  Bit Score: 523.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   1 MAIFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPK 80
Cdd:PRK05678    1 MSILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVL----GLPVFNTVAEAVEATGANASVIYVPPP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  81 FTKDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKS 160
Cdd:PRK05678   77 FAADAILEAIDAGIDLIVCITEGIPVLDMLEVKAYL--ERKKTRLIGPNCPGIITPGECKIGIMPGHIHKKGRVGVVSRS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 161 GTLTYQLMYELRDIGF--SSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVTKPVVGYV 238
Cdd:PRK05678  155 GTLTYEAVAQLTDLGFgqSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKANVTKPVVGYI 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021337389 239 AGFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREIIAG 294
Cdd:PRK05678  235 AGVTAPPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKG 290
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 2-293 1.26e-170

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


Pssm-ID: 439844 [Multi-domain]  Cd Length: 288  Bit Score: 473.78  E-value: 1.26e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   2 AIFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPKF 81
Cdd:COG0074     1 SILVNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGQTVL----GVPVFDTVAEAVEETGADASVIFVPPPF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  82 TKDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKSG 161
Cdd:COG0074    77 AADAILEAIDAGIKLIVCITEGIPVLDMVRVKRYA--KAKGTRLIGPNCPGIITPGECKLGIMPGHIFKPGRVGIVSRSG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 162 TLTYQLMYELRD--IGFSSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVTKPVVGYVA 239
Cdd:COG0074   155 TLTYEAVWQLTQagLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIKENMTKPVVAYIA 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1021337389 240 GFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREIIA 293
Cdd:COG0074   235 GRTAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKALK 288
sucCoAalpha TIGR01019
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ...
 3-292 1.84e-147

succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]


Pssm-ID: 130091 [Multi-domain]  Cd Length: 286  Bit Score: 414.89  E-value: 1.84e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   3 IFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVdvdgTEVPVFGGVAEAMEKTGADVTVIFVPPKFT 82
Cdd:TIGR01019   1 ILLDKDTKVIVQGITGSQGSFHTEQMLAYGTNIVGGVTPGKGGTTV----LGLPVFDSVKEAVEETGANASVIFVPAPFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  83 KDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKSGT 162
Cdd:TIGR01019  77 ADAIFEAIDAGIELIVCITEGIPVHDMLKVKRYM--EESGTRLIGPNCPGIITPGECKIGIMPGHIHKPGNVGIVSRSGT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 163 LTYQLMYELRDIGF--SSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVTKPVVGYVAG 240
Cdd:TIGR01019 155 LTYEAVHQLTKAGFgqSTCVGIGGDPVNGTSFIDVLEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQNMSKPVVGFIAG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1021337389 241 FTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREII 292
Cdd:TIGR01019 235 ATAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVTVVKSPSDIGELLAEIL 286
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 4-104 1.97e-26

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 99.51  E-value: 1.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389    4 FLTKDSKVIVQGMTGSEGMKHTRRM---LASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPK 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMrnlLEYGTKFVGGVYPGKVGPKVD----GVPVYDSVAEAPEETGVDVAVIFVPAE 76

                           90       100
                   ....*....|....*....|....
gi 1021337389   81 FTKDAVVEAIDAEIGLAVVITEGV 104
Cdd:smart00881  77 AAPDAIDEAIEAGIKGIVVITEGI 100
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 6-103 8.87e-26

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 98.05  E-value: 8.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   6 TKDSKVIVQGMTGS---EGMKHTRRMLASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPKFT 82
Cdd:pfam02629   1 DKDTKVIVIGAGGLgiqGLNYHFIQMLGYGIKMVFGVNPGKGGTEIL----GIPVYNSVDELEEKTGVDVAVITVPAPFA 76

                          90       100
                  ....*....|....*....|.
gi 1021337389  83 KDAVVEAIDAEIGLAVVITEG 103
Cdd:pfam02629  77 QEAIDELVDAGIKGIVNITPG 97
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 10-99 2.02e-03

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 37.91  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  10 KVIVQGMtGSEGMKHTRRMLAS-GTQIVGGV--NPRKAGTTVDV----DGTEVPVFGGVAEAMEKTGADVTVIFVPPKFT 82
Cdd:cd24146     2 RVVVWGL-GAMGRGIARYLLEKpGLEIVGAVdrDPAKVGKDLGElgggAPLGVKVTDDLDAVLAATKPDVVVHATTSFLA 80

                          90
                  ....*....|....*....
gi 1021337389  83 K--DAVVEAIDAeiGLAVV 99
Cdd:cd24146    81 DvaPQIERLLEA--GLNVI 97
 
Name Accession Description Interval E-value
PRK05678 PRK05678
succinyl-CoA synthetase subunit alpha; Validated
 1-294 0e+00

succinyl-CoA synthetase subunit alpha; Validated


Pssm-ID: 180194 [Multi-domain]  Cd Length: 291  Bit Score: 523.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   1 MAIFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPK 80
Cdd:PRK05678    1 MSILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVL----GLPVFNTVAEAVEATGANASVIYVPPP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  81 FTKDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKS 160
Cdd:PRK05678   77 FAADAILEAIDAGIDLIVCITEGIPVLDMLEVKAYL--ERKKTRLIGPNCPGIITPGECKIGIMPGHIHKKGRVGVVSRS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 161 GTLTYQLMYELRDIGF--SSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVTKPVVGYV 238
Cdd:PRK05678  155 GTLTYEAVAQLTDLGFgqSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKANVTKPVVGYI 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021337389 239 AGFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREIIAG 294
Cdd:PRK05678  235 AGVTAPPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKG 290
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 2-293 1.26e-170

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


Pssm-ID: 439844 [Multi-domain]  Cd Length: 288  Bit Score: 473.78  E-value: 1.26e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   2 AIFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPKF 81
Cdd:COG0074     1 SILVNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGQTVL----GVPVFDTVAEAVEETGADASVIFVPPPF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  82 TKDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKSG 161
Cdd:COG0074    77 AADAILEAIDAGIKLIVCITEGIPVLDMVRVKRYA--KAKGTRLIGPNCPGIITPGECKLGIMPGHIFKPGRVGIVSRSG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 162 TLTYQLMYELRD--IGFSSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVTKPVVGYVA 239
Cdd:COG0074   155 TLTYEAVWQLTQagLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIKENMTKPVVAYIA 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1021337389 240 GFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREIIA 293
Cdd:COG0074   235 GRTAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKALK 288
sucCoAalpha TIGR01019
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ...
 3-292 1.84e-147

succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]


Pssm-ID: 130091 [Multi-domain]  Cd Length: 286  Bit Score: 414.89  E-value: 1.84e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   3 IFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVdvdgTEVPVFGGVAEAMEKTGADVTVIFVPPKFT 82
Cdd:TIGR01019   1 ILLDKDTKVIVQGITGSQGSFHTEQMLAYGTNIVGGVTPGKGGTTV----LGLPVFDSVKEAVEETGANASVIFVPAPFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  83 KDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKSGT 162
Cdd:TIGR01019  77 ADAIFEAIDAGIELIVCITEGIPVHDMLKVKRYM--EESGTRLIGPNCPGIITPGECKIGIMPGHIHKPGNVGIVSRSGT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 163 LTYQLMYELRDIGF--SSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVTKPVVGYVAG 240
Cdd:TIGR01019 155 LTYEAVHQLTKAGFgqSTCVGIGGDPVNGTSFIDVLEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQNMSKPVVGFIAG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1021337389 241 FTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREII 292
Cdd:TIGR01019 235 ATAPPGKRMGHAGAIISGGKGTAESKIEALEAAGVTVVKSPSDIGELLAEIL 286
PTZ00187 PTZ00187
succinyl-CoA synthetase alpha subunit; Provisional
 3-292 6.31e-119

succinyl-CoA synthetase alpha subunit; Provisional


Pssm-ID: 240307 [Multi-domain]  Cd Length: 317  Bit Score: 344.01  E-value: 6.31e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   3 IFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTVDVDGteVPVFGGVAEAMEKTGADVTVIFVPPKFT 82
Cdd:PTZ00187   24 VWVNKNTKVICQGITGKQGTFHTEQAIEYGTKMVGGVNPKKAGTTHLKHG--LPVFATVKEAKKATGADASVIYVPPPHA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  83 KDAVVEAIDAEIGLAVVITEGVPVHDTAAFwAYAGSKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKSGT 162
Cdd:PTZ00187  102 ASAIIEAIEAEIPLVVCITEGIPQHDMVKV-KHALLSQNKTRLIGPNCPGIIKPGECKIGIMPGHIHKKGKIGIVSRSGT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 163 LTYQLMYELRDIGF--SSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVT-KPVVGYVA 239
Cdd:PTZ00187  181 LTYEAVAQTTAVGLgqSTCVGIGGDPFNGTNFIDCLKLFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIkKPVVSFIA 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1021337389 240 GFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSETARLAREII 292
Cdd:PTZ00187  261 GITAPPGRRMGHAGAIISGGKGTAPGKIEALEAAGVRVVKSPAQLGKTMLEVM 313
PLN00125 PLN00125
Succinyl-CoA ligase [GDP-forming] subunit alpha
 2-283 4.08e-96

Succinyl-CoA ligase [GDP-forming] subunit alpha


Pssm-ID: 215066 [Multi-domain]  Cd Length: 300  Bit Score: 285.32  E-value: 4.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   2 AIFLTKDSKVIVQGMTGSEGMKHTRRMLASGTQIVGGVNPRKAGTTvdvdGTEVPVFGGVAEAMEKTGADVTVIFVPPKF 81
Cdd:PLN00125    6 AVFVDKNTRVICQGITGKNGTFHTEQAIEYGTKMVGGVTPKKGGTE----HLGLPVFNTVAEAKAETKANASVIYVPPPF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  82 TKDAVVEAIDAEIGLAVVITEGVPVHDTAAFWAyAGSKGNKTRIIGPNCPGLISPGQSNAGIIPADITTSGKIGLVSKSG 161
Cdd:PLN00125   82 AAAAILEAMEAELDLVVCITEGIPQHDMVRVKA-ALNRQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGRIGIVSRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 162 TLTYQLMYELRDIGF--SSAVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGGDAEERAAAYIAEHVT-KPVVGYV 238
Cdd:PLN00125  161 TLTYEAVFQTTAVGLgqSTCVGIGGDPFNGTNFVDCLEKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTeKPVVAFI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1021337389 239 AGFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGVKVGKTPSE 283
Cdd:PLN00125  241 AGLTAPPGRRMGHAGAIVSGGKGTAQDKIKALREAGVTVVESPAK 285
PLN02522 PLN02522
ATP citrate (pro-S)-lyase
 35-277 4.80e-29

ATP citrate (pro-S)-lyase


Pssm-ID: 178137 [Multi-domain]  Cd Length: 608  Bit Score: 116.07  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  35 IVGGVNPRKAGTTVDVDGTE---VPVFGGVAEAMEK-TGADVTVIFVPPKFTKDAVVEAIDAE-IGLAVVITEGVPVHDT 109
Cdd:PLN02522   40 VAGIINPGSEGFQKLFFGQEeiaIPVHGSIEAACKAhPTADVFINFASFRSAAASSMEALKQPtIRVVAIIAEGVPESDT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 110 AAFWAYAgsKGNKTRIIGPNCPGLISPGQSNAG--------IIPADITTSGKIGLVSKSGTLT---YQLMYELRDiGFSS 178
Cdd:PLN02522  120 KQLIAYA--RANNKVVIGPATVGGIQAGAFKIGdtagtldnIIQCKLYRPGSVGFVSKSGGMSnemYNVIARVTD-GIYE 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 179 AVGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIGG-DAEERAAAYIAEHVTKPVVGYVAGFTAPEGKT---MGHAGA 254
Cdd:PLN02522  197 GIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGrDEYSLVEALKQGKVSKPVVAWVSGTCARLFKSevqFGHAGA 276

                         250       260
                  ....*....|....*....|...
gi 1021337389 255 IVSGSSGTAQAKKEALEAAGVKV 277
Cdd:PLN02522  277 KSGGDMESAQAKNKALKDAGAIV 299
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 4-104 1.97e-26

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 99.51  E-value: 1.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389    4 FLTKDSKVIVQGMTGSEGMKHTRRM---LASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPK 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMrnlLEYGTKFVGGVYPGKVGPKVD----GVPVYDSVAEAPEETGVDVAVIFVPAE 76

                           90       100
                   ....*....|....*....|....
gi 1021337389   81 FTKDAVVEAIDAEIGLAVVITEGV 104
Cdd:smart00881  77 AAPDAIDEAIEAGIKGIVVITEGI 100
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 6-103 8.87e-26

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 98.05  E-value: 8.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389   6 TKDSKVIVQGMTGS---EGMKHTRRMLASGTQIVGGVNPRKAGTTVDvdgtEVPVFGGVAEAMEKTGADVTVIFVPPKFT 82
Cdd:pfam02629   1 DKDTKVIVIGAGGLgiqGLNYHFIQMLGYGIKMVFGVNPGKGGTEIL----GIPVYNSVDELEEKTGVDVAVITVPAPFA 76

                          90       100
                  ....*....|....*....|.
gi 1021337389  83 KDAVVEAIDAEIGLAVVITEG 103
Cdd:pfam02629  77 QEAIDELVDAGIKGIVNITPG 97
Ligase_CoA pfam00549
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ...
 157-275 2.46e-21

CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.


Pssm-ID: 395434 [Multi-domain]  Cd Length: 128  Bit Score: 87.31  E-value: 2.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 157 VSKSGTLTYQLMYELRDIGFSSA--VGIGGDPVIGTTHIDALKAFQEDPETELIVMIGEIG-GDAEERAAAYIAEH---- 229
Cdd:pfam00549   1 LVNGGTLAMEAMDLIKLAGGGPHnfIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPAGGLLKAIkear 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1021337389 230 -VTKPVVGYVAGFTAPEGKTMGHAGAIVSGSSGTAQAKKEALEAAGV 275
Cdd:pfam00549  81 aRELPVVARVCGTEADPQGRSGQAKALAESGVLIASSNNQALRAAGA 127
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
71-275 1.44e-15

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 76.70  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  71 DVTVIFVPPKFTKDAVVEAIDAEIGLAVVIT--------EGVP----VHDTAafwayagsKGNKTRIIGPNCPGLISPGQ 138
Cdd:COG1042    71 DLAVIAVPAETVPDVVEECGEKGVKAAVVISagfaetgeEGAAleqeLLEIA--------RRYGMRLLGPNCLGLINPAT 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 139 S-NAGIIPADItTSGKIGLVSKSGTLTYQLMYEL--RDIGFSSAVGIGGDPVIGTThiDALKAFQEDPETELIVMIGEIG 215
Cdd:COG1042   143 GlNATFAPVPP-LPGNIALVSQSGALGTAILDWAaaRGIGFSHFVSLGNEADVDFA--DLLDYLADDPDTRVILLYLEGI 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021337389 216 GDAEE-----RAAAYiaehvTKPVVGYVAGfTAPEGK--TMGHAGAIVsGSSGTAQAkkeALEAAGV 275
Cdd:COG1042   220 RDGRRflsaaRAAAR-----GKPVVVLKSG-RSEAGAraAASHTGALA-GSDAVYDA---AFRRAGV 276
Succ_CoA_lig pfam13607
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ...
 152-289 3.17e-10

Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from Succinyl-CoA ligase alpha subunit and other related enzymes. A conserved histidine is involved in phosphoryl transfer.


Pssm-ID: 433345 [Multi-domain]  Cd Length: 138  Bit Score: 57.09  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 152 GKIGLVSKSGTLTYQLMYEL--RDIGFSSAVGIGGDPVIGTThiDALKAFQEDPETELIVMIGEIGGDAEE--RAAAYIA 227
Cdd:pfam13607   2 GNIALVSQSGALGAALLDWArsRGIGFSKFVSLGNEADVDFA--DLLEYLADDPETRVILLYLEGIRDGRRflRAARRAA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021337389 228 EHvtKPVVGYVAGfTAPEGK--TMGHAGAIvSGSSGTAQAkkeALEAAGVKVGKTPSETARLAR 289
Cdd:pfam13607  80 RR--KPVVVLKAG-RSEAGAraAASHTGAL-AGSDAVYDA---AFRQAGVIRVDDLEELFDAAE 136
PRK06091 PRK06091
membrane protein FdrA; Validated
 64-290 4.16e-08

membrane protein FdrA; Validated


Pssm-ID: 180395 [Multi-domain]  Cd Length: 555  Bit Score: 53.90  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  64 AMEKT-GADVTVIFVPPKFTKDAVVEAIDAeiGLAVVI-TEGVPVHDTAAFWAYAGSKGnkTRIIGPNCpglispGQSNA 141
Cdd:PRK06091  111 ACQKLpDANLALISVAGEYAAELAEQALDR--NLNVMMfSDNVTLEDEIRLKTRAREKG--LLVMGPDC------GTAMI 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 142 GIIP---ADITTSGKIGLVSKSGT----LTYQLmyELRDIGFSSAVGIGG----DPVIGTTHIDALKAFQEDPETELIVM 210
Cdd:PRK06091  181 AGTPlafANVMPEGNIGVIGASGTgiqeLCSQI--ALAGEGITHAIGLGGrdlsAEVGGISALTALEMLSADEKSEVIAF 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389 211 IGEIGGDAEERAAAYIAEHVTKPVVGYVAGFTAP---EG-----KTMGHAGAIVSGSSGTAQAKKEALEAAGVKV----- 277
Cdd:PRK06091  259 VSKPPAEAVRLKIINAMKATGKPVVALFLGYTPAvarDEnvwfaSTLDEAARLACLLSRVTAQRNAILPVSQGFIcglyt 338

                         250
                  ....*....|....
gi 1021337389 278 -GKTPSETARLARE 290
Cdd:PRK06091  339 gGTLAAEAAGLLAG 352
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 26-136 4.68e-05

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 41.76  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  26 RRMLASGTQIVGgVNPRKAgttvDVDGteVPVFGGVAEAMEKtgADVTVIFVPPKFTKDAVVEAIDAEIGlAVVITEGVp 105
Cdd:pfam13380  21 RYLLEHGYPVIP-VNPKAK----EILG--EPVYPSLADPPEP--VDLVDVFRPPEAVPEIVEEALALGAK-AVWLQPGI- 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1021337389 106 VHDTAAfwAYAGSKGNktRIIGPNCPGLISP 136
Cdd:pfam13380  90 ENEEAA--AIARAAGI--RVVGDRCLGVEHP 116
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 10-99 2.02e-03

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 37.91  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021337389  10 KVIVQGMtGSEGMKHTRRMLAS-GTQIVGGV--NPRKAGTTVDV----DGTEVPVFGGVAEAMEKTGADVTVIFVPPKFT 82
Cdd:cd24146     2 RVVVWGL-GAMGRGIARYLLEKpGLEIVGAVdrDPAKVGKDLGElgggAPLGVKVTDDLDAVLAATKPDVVVHATTSFLA 80

                          90
                  ....*....|....*....
gi 1021337389  83 K--DAVVEAIDAeiGLAVV 99
Cdd:cd24146    81 DvaPQIERLLEA--GLNVI 97
 
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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