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Conserved domains on  [gi|2284063064|pdb|7PCL|B]
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Chain B, Ketol-acid reductoisomerase

Protein Classification

ketol-acid reductoisomerase( domain architecture ID 1005095)

ketol-acid reductoisomerase (KARI) catalyzes the conversion of acetohydroxy acids into dihydroxy valerates, which is the second reaction in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine

CATH:  1.10.1040.10|3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0004455|GO:0046872|GO:0016491
PubMed:  25172159
SCOP:  4000106

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IlvC super family cl33753
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 10-332 6.71e-81

Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


The actual alignment was detected with superfamily member COG0059:

Pssm-ID: 439829 [Multi-domain]  Cd Length: 328  Bit Score: 249.98  E-value: 6.71e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       10 IYQDEHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDR-YFELARAEGHRVTNIAEAVAHADIVLLLIPD 88
Cdd:COG0059   4 IYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSkSWKKAEEDGFEVMTVAEAAKRADVIMILTPD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       89 EAHGAVFDVDIAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARD 168
Cdd:COG0059  84 EVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGKAKD 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B      169 RVLAIARAVGFTRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLEVYG----------SGE 237
Cdd:COG0059 164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQaVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHelklivdliyEGG 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B      238 MGKMML---DGADIGldevvALQGSPtcqvgyhrwrgRTLPTAVRELAARVLDQIEGGDFSA-YLKEQAsNDYASLDDAR 313
Cdd:COG0059 244 IANMRYsisNTAEYG-----DYTRGP-----------RVITEEVKEEMKKVLDDIQSGEFAKeWILENQ-AGRPNLNALR 306

                       330
                ....*....|....*....
7PCL_B      314 RAALKRPLNVAHAQVRAAF 332
Cdd:COG0059 307 AEEAEHPIEKVGAELRAMM 325
 
Name Accession Description Interval E-value
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 10-332 6.71e-81

Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439829 [Multi-domain]  Cd Length: 328  Bit Score: 249.98  E-value: 6.71e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       10 IYQDEHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDR-YFELARAEGHRVTNIAEAVAHADIVLLLIPD 88
Cdd:COG0059   4 IYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSkSWKKAEEDGFEVMTVAEAAKRADVIMILTPD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       89 EAHGAVFDVDIAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARD 168
Cdd:COG0059  84 EVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGKAKD 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B      169 RVLAIARAVGFTRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLEVYG----------SGE 237
Cdd:COG0059 164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQaVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHelklivdliyEGG 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B      238 MGKMML---DGADIGldevvALQGSPtcqvgyhrwrgRTLPTAVRELAARVLDQIEGGDFSA-YLKEQAsNDYASLDDAR 313
Cdd:COG0059 244 IANMRYsisNTAEYG-----DYTRGP-----------RVITEEVKEEMKKVLDDIQSGEFAKeWILENQ-AGRPNLNALR 306

                       330
                ....*....|....*....
7PCL_B      314 RAALKRPLNVAHAQVRAAF 332
Cdd:COG0059 307 AEEAEHPIEKVGAELRAMM 325
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 10-232 1.45e-69

ketol-acid reductoisomerase; Provisional


Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 220.73  E-value: 1.45e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        10 IYQDEHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVG-NIDDRYFELARAEGHRVTNIAEAVAHADIVLLLIPD 88
Cdd:PRK05479   4 VYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGlREGSKSWKKAEADGFEVLTVAEAAKWADVIMILLPD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        89 EAHGAVFDVDIAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARD 168
Cdd:PRK05479  84 EVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGNAKD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
7PCL_B       169 RVLAIARAVGFTRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLEV 232
Cdd:PRK05479 164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQaVLCGGLTELIKAGFETLVEAGYQPEMAYFEC 228
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 21-315 9.15e-56

ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 273093 [Multi-domain]  Cd Length: 314  Bit Score: 184.89  E-value: 9.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B         21 LEGRTVAVIGYGIQGRAFAANLRDSGVAVRVG-NIDDRYFELARAEGHRVTNIAEAVAHADIVLLLIPDEAHGAVFDVDI 99
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGlRKGGASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        100 APNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARDRVLAIARAVGF 179
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        180 TRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLE-VYGSGEMGKMMLDGADIGLDEVValq 257
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQaVLCGGLTALIKAGFDTLVEAGYQPELAYFEtVHELKLIVDLIYEGGITGMRDRI--- 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
7PCL_B        258 gSPTCQVGYHRWRgRTLPTAVRELAARVLDQIEGGDFSAYLKEQASNDYASLDDARRA 315
Cdd:TIGR00465 238 -SNTAEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKY 293
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 20-183 3.35e-55

Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.


Pssm-ID: 285265  Cd Length: 165  Bit Score: 178.12  E-value: 3.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B         20 PLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDD-RYFELARAEGHRVTNIAEAVAHADIVLLLIPDEAHGAVFDVD 98
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B         99 IAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARDRVLAIARAVG 178
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160


                  ....*
7PCL_B        179 FTRAG 183
Cdd:pfam07991 161 GTRAG 165
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
23-116 4.63e-09

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 54.76  E-value: 4.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B          23 GRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHRVTNIAEAVAHADIVLllipdEAHG--AVFDVDIA 100
Cdd:smart00997  23 GKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRADIFV-----TATGnkDVITREHF 97

                           90
                   ....*....|....*.
7PCL_B         101 PNLRDGALLCVAhGHS 116
Cdd:smart00997  98 RAMKDGAILANA-GHF 112
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 23-125 2.18e-06

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619 [Multi-domain]  Cd Length: 402  Bit Score: 48.99  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       23 GRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDD-RYFElARAEGHRVTNIAEAVAHADIVLllipdEAHG--AVFDVDI 99
Cdd:cd00401 195 GKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPiCALQ-AAMDGFEVMPMEEAAKIGDIFV-----TATGnkDVIRGEH 268

                        90       100
                ....*....|....*....|....*.
7PCL_B      100 APNLRDGALLCVAhGHSLVQGDVRPL 125
Cdd:cd00401 269 FEKMKDGAILCNA-GHFDVEIDVAAL 293
 
Name Accession Description Interval E-value
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 10-332 6.71e-81

Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439829 [Multi-domain]  Cd Length: 328  Bit Score: 249.98  E-value: 6.71e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       10 IYQDEHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDR-YFELARAEGHRVTNIAEAVAHADIVLLLIPD 88
Cdd:COG0059   4 IYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSkSWKKAEEDGFEVMTVAEAAKRADVIMILTPD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       89 EAHGAVFDVDIAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARD 168
Cdd:COG0059  84 EVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGKAKD 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B      169 RVLAIARAVGFTRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLEVYG----------SGE 237
Cdd:COG0059 164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQaVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHelklivdliyEGG 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B      238 MGKMML---DGADIGldevvALQGSPtcqvgyhrwrgRTLPTAVRELAARVLDQIEGGDFSA-YLKEQAsNDYASLDDAR 313
Cdd:COG0059 244 IANMRYsisNTAEYG-----DYTRGP-----------RVITEEVKEEMKKVLDDIQSGEFAKeWILENQ-AGRPNLNALR 306

                       330
                ....*....|....*....
7PCL_B      314 RAALKRPLNVAHAQVRAAF 332
Cdd:COG0059 307 AEEAEHPIEKVGAELRAMM 325
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 10-232 1.45e-69

ketol-acid reductoisomerase; Provisional


Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 220.73  E-value: 1.45e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        10 IYQDEHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVG-NIDDRYFELARAEGHRVTNIAEAVAHADIVLLLIPD 88
Cdd:PRK05479   4 VYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGlREGSKSWKKAEADGFEVLTVAEAAKWADVIMILLPD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        89 EAHGAVFDVDIAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARD 168
Cdd:PRK05479  84 EVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGNAKD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
7PCL_B       169 RVLAIARAVGFTRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLEV 232
Cdd:PRK05479 164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQaVLCGGLTELIKAGFETLVEAGYQPEMAYFEC 228
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 21-315 9.15e-56

ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 273093 [Multi-domain]  Cd Length: 314  Bit Score: 184.89  E-value: 9.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B         21 LEGRTVAVIGYGIQGRAFAANLRDSGVAVRVG-NIDDRYFELARAEGHRVTNIAEAVAHADIVLLLIPDEAHGAVFDVDI 99
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGlRKGGASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        100 APNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARDRVLAIARAVGF 179
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        180 TRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLE-VYGSGEMGKMMLDGADIGLDEVValq 257
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQaVLCGGLTALIKAGFDTLVEAGYQPELAYFEtVHELKLIVDLIYEGGITGMRDRI--- 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
7PCL_B        258 gSPTCQVGYHRWRgRTLPTAVRELAARVLDQIEGGDFSAYLKEQASNDYASLDDARRA 315
Cdd:TIGR00465 238 -SNTAEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKY 293
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 20-183 3.35e-55

Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.


Pssm-ID: 285265  Cd Length: 165  Bit Score: 178.12  E-value: 3.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B         20 PLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDD-RYFELARAEGHRVTNIAEAVAHADIVLLLIPDEAHGAVFDVD 98
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B         99 IAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARDRVLAIARAVG 178
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160


                  ....*
7PCL_B        179 FTRAG 183
Cdd:pfam07991 161 GTRAG 165
PRK13403 PRK13403
ketol-acid reductoisomerase; Provisional
 11-295 4.16e-54

ketol-acid reductoisomerase; Provisional


Pssm-ID: 106361 [Multi-domain]  Cd Length: 335  Bit Score: 181.10  E-value: 4.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        11 YQDEHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHRVTNIAEAVAHADIVLLLIPDEA 90
Cdd:PRK13403   4 YYEKDANVELLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGKSFEVAKADGFEVMSVSEAVRTAQVVQMLLPDEQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        91 HGAVFDVDIAPNLRDGALLCVAHGHSLVQGDVRPLPGRDLAMLAPRMYGDPIRRYYLAGQGAPAYFDIVADHTGRARDRV 170
Cdd:PRK13403  84 QAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALHVA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       171 LAIARAVGFTRAGVMALGYRQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLEVYGSGEM-GKMMLDGADI 248
Cdd:PRK13403 164 LAYAKGVGCTRAGVIETTFQEETETDLFGEQaVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLiVDLMYEGGLT 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
7PCL_B       249 GLDEVValqgSPTCQVGYHRWRGRTLPTAVRELAARVLDQIEGGDFS 295
Cdd:PRK13403 244 NMRHSI----SDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFA 286
IlvC pfam01450
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ...
 190-329 5.87e-24

Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine.


Pssm-ID: 460215 [Multi-domain]  Cd Length: 138  Bit Score: 95.61  E-value: 5.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        190 RQETFLDLFQEQ-FLAPALVDLVETGFQVLVERGFNPKAALLEVYGsgEMgKMMLDG-ADIGLDeVVALQGSPTCQVGYH 267
Cdd:pfam01450   1 KEETETDLFGEQaVLCGGVTGLVKAGFETLVEAGYQPEAAYFECLH--EL-KLIVDLiYEGGIA-GMRYSISDTAEYGDL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
7PCL_B        268 RWRGRTLPTAVRELAARVLDQIEGGDF-SAYLKEQAsNDYASLDDARRAALKRPLNVAHAQVR 329
Cdd:pfam01450  77 TRGPRVIYDATKELMKEILDEIQSGEFaKEWILEYQ-AGRPELKALRREEAEHPIEKVGKELR 138
PRK05225 PRK05225
ketol-acid reductoisomerase; Validated
 21-234 2.55e-14

ketol-acid reductoisomerase; Validated


Pssm-ID: 235368 [Multi-domain]  Cd Length: 487  Bit Score: 73.84  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        21 LEGRTVAVIGYGIQGRAFAANLRDSGV----AVRVGNIDDRYFELARA--EGHRVTNIAEAVAHADIVLLLIPDEAHGAV 94
Cdd:PRK05225  34 LKGKKIVIVGCGAQGLNQGLNMRDSGLdisyALRKEAIAEKRASWRKAteNGFKVGTYEELIPQADLVINLTPDKQHSDV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        95 FDvDIAPNLRDGALLCVAHGHSLVQ-GD-VRPlpgrDLA--MLAPRMYGDPIRRYYLAGQGAPAyfdIVA-----DHTGR 165
Cdd:PRK05225 114 VR-AVQPLMKQGAALGYSHGFNIVEvGEqIRK----DITvvMVAPKCPGTEVREEYKRGFGVPT---LIAvhpenDPKGE 185

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7PCL_B       166 ARDRVLAIARAVGFTRAGVMALGYRQETFLDLFQEQFLapaLVDLVETG----FQVLVERGFNPK-AALLEVYG 234
Cdd:PRK05225 186 GMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTI---LCGMLQAGsllcFDKLVAEGTDPAyAEKLIQFG 256
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
23-116 4.63e-09

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 54.76  E-value: 4.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B          23 GRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHRVTNIAEAVAHADIVLllipdEAHG--AVFDVDIA 100
Cdd:smart00997  23 GKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRADIFV-----TATGnkDVITREHF 97

                           90
                   ....*....|....*.
7PCL_B         101 PNLRDGALLCVAhGHS 116
Cdd:smart00997  98 RAMKDGAILANA-GHF 112
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 25-109 3.32e-08

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 53.97  E-value: 3.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       25 TVAVIGYGIQGRAFAANLRDSGVAVRVGNID-DRYFELARAEGHRVTNIAEAVAHADIVLLLIPDEAH--GAVFDVD-IA 100
Cdd:COG2084   3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTpAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAveEVLLGEDgLL 82


                ....*....
7PCL_B      101 PNLRDGALL 109
Cdd:COG2084  83 AALRPGAVV 91
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 25-109 3.87e-08

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 52.09  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B         25 TVAVIGYGIQGRAFAANLRDSGVAVRVGNID-DRYFELARAEGHRVTNIAEAVAHADIVLLLIPDEAH--GAVFDVDIAP 101
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTpEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAvdAVIFGEGLLP 80


                  ....*...
7PCL_B        102 NLRDGALL 109
Cdd:pfam03446  81 GLKPGDII 88
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 20-109 2.41e-07

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 52.69  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        20 PLEGRtVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHRV-----TNIAEAVAHADIVLLLIPDEAHGAV 94
Cdd:PRK14806   1 PLFGR-VVVIGLGLIGGSFAKALRERGLAREVVAVDRRAKSLELAVSLGVidrgeEDLAEAVSGADVIVLAVPVLAMEKV 79

                         90
                 ....*....|....*
7PCL_B        95 FdVDIAPNLRDGALL 109
Cdd:PRK14806  80 L-ADLKPLLSEHAIV 93
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
24-109 1.09e-06

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 49.58  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B        24 RTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAE----GHRVT-NIAEAVAHADIVLLLIPDEAHGAVfDVD 98
Cdd:PRK07502   7 DRVALIGIGLIGSSLARAIRRLGLAGEIVGADRSAETRARARelglGDRVTtSAAEAVKGADLVILCVPVGASGAV-AAE 85

                         90
                 ....*....|.
7PCL_B        99 IAPNLRDGALL 109
Cdd:PRK07502  86 IAPHLKPGAIV 96
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 23-125 2.18e-06

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619 [Multi-domain]  Cd Length: 402  Bit Score: 48.99  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       23 GRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDD-RYFElARAEGHRVTNIAEAVAHADIVLllipdEAHG--AVFDVDI 99
Cdd:cd00401 195 GKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPiCALQ-AAMDGFEVMPMEEAAKIGDIFV-----TATGnkDVIRGEH 268

                        90       100
                ....*....|....*....|....*.
7PCL_B      100 APNLRDGALLCVAhGHSLVQGDVRPL 125
Cdd:cd00401 269 FEKMKDGAILCNA-GHFDVEIDVAAL 293
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
27-94 1.38e-04

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 40.29  E-value: 1.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7PCL_B         27 AVIGYGIQGRAFAANLRDSGVA-VRVGNI--DDRYFELARAEGHRVT--NIAEAVAHADIVLLLIPDEAHGAV 94
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHeVVVANSrnPEKAEELAEEYGVGATavDNEEAAEEADVVFLAVKPEDAPDV 73
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 21-92 1.47e-04

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 42.10  E-value: 1.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7PCL_B         21 LEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHRVTNIAEAVAHADIVLLLIP--DEAHG 92
Cdd:pfam02826  34 LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVSLHLPltPETRH 107
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 21-122 1.62e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 43.05  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       21 LEGRTVAVIGYGIQGRAFAANLRDSGVAVRVgniDDRYFELARAEGHRVTnIAEAVAHADIVLLLIP--DEAHGAVFDVD 98
Cdd:cd12179 136 LMGKTVGIIGYGNMGKAFAKRLSGFGCKVIA---YDKYKNFGDAYAEQVS-LETLFKEADILSLHIPltPETRGMVNKEF 211

                        90       100
                ....*....|....*....|....
7PCL_B       99 IAPNLRDGALLCVAHGHSLVQGDV 122
Cdd:cd12179 212 ISSFKKPFYFINTARGKVVVTKDL 235
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 24-109 1.67e-04

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 42.81  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       24 RTVAVIGYGIQGRAFAANLRDSGVAVRV-G-NIDDRYFELARAEG--HRV-TNIAEAVAHADIVLLLIPDEAHGAVFDvD 98
Cdd:COG0287   2 MRIAIIGLGLIGGSLALALKRAGLAHEVvGvDRSPETLERALELGviDRAaTDLEEAVADADLVVLAVPVGATIEVLA-E 80

                        90
                ....*....|.
7PCL_B       99 IAPNLRDGALL 109
Cdd:COG0287  81 LAPHLKPGAIV 91
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 14-109 1.78e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 42.96  E-value: 1.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       14 EHASLQPLEGRTVAVIGYGIQGRAFAANLRDSGVAV-RVGNIddryfelARAEG--HRVTNIAEAVAHADIVLLLIP--D 88
Cdd:cd12166 123 EPRRTPSLADRRVLIVGYGSIGRAIERRLAPFEVRVtRVART-------ARPGEqvHGIDELPALLPEADVVVLIVPltD 195

                        90       100
                ....*....|....*....|.
7PCL_B       89 EAHGAVfDVDIAPNLRDGALL 109
Cdd:cd12166 196 ETRGLV-DAEFLARMPDGALL 215
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
26-198 2.03e-04

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 42.08  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       26 VAVIGYGIQGRAFAANLRDSGVAVRVGNID-DRYFELARAEGHRVT--NIAEAVAHADIVLLLIPDEAHGAVFDvDIAPN 102
Cdd:COG2085   1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDpEKAAALAAELGPGARagTNAEAAAAADVVVLAVPYEAVPDVLE-SLGDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B      103 L--------------RDGALLCVAHGHS---LVQgdvRPLPGRDL-----AMLAPRMYGDPirryyLAGQGAPAYFdIVA 160
Cdd:COG2085  80 LagkividatnplpeRDGFILDPPGGGSaaeLVA---ALLPGARVvkafnTIGAAVLADPA-----RPAGGRRDVF-VAG 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
7PCL_B      161 DHTGrARDRVLAIARAVGFT--RAGVMALGYRQETFLDLF 198
Cdd:COG2085 151 DDAE-AKAVVAALIEDLGFDpvDAGPLANARRLEPLTPLL 189
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 21-114 5.71e-04

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 41.45  E-value: 5.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       21 LEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHR-VTNIAEAVAHADIVLL--LIPDEAHGAVFDV 97
Cdd:cd12154 158 VAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKnVEELEEALAEADVIVTttLLPGKRAGILVPE 237

                        90
                ....*....|....*...
7PCL_B       98 DIAPNLRDGALLC-VAHG 114
Cdd:cd12154 238 ELVEQMKPGSVIVnVAVG 255
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 12-114 1.26e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 40.30  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       12 QDEHASLQpleGRTVAVIGYGIQGRAFAANLRDSGVAV----RVGNIDDryfelARAEGHRVTNIAEAVAHADIVLLLIP 87
Cdd:cd12165 129 EPESKELR---GKTVGILGYGHIGREIARLLKAFGMRVigvsRSPKEDE-----GADFVGTLSDLDEALEQADVVVVALP 200

                        90       100       110
                ....*....|....*....|....*....|
7PCL_B       88 --DEAHGaVFDVDIAPNLRDGALL-CVAHG 114
Cdd:cd12165 201 ltKQTRG-LIGAAELAAMKPGAILvNVGRG 229
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 21-81 1.27e-03

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 40.41  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
7PCL_B        21 LEGRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHRVTNIAEAVAHADI 81
Cdd:PTZ00075 252 IAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADI 312
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 24-109 1.36e-03

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 40.05  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B       24 RTVAVIGYGIQGRAFAANLRDSGVA---VRVGNID-DRYFELARAEG-HRVTNIAEAVAHADIVLLLIPDEAHGAVFDvD 98
Cdd:COG0345   3 MKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSpERLEALAERYGvRVTTDNAEAAAQADVVVLAVKPQDLAEVLE-E 81

                        90
                ....*....|.
7PCL_B       99 IAPNLRDGALL 109
Cdd:COG0345  82 LAPLLDPDKLV 92
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
23-110 2.53e-03

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 39.45  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7PCL_B          23 GRTVAVIGYGIQGRAFAANLRDSGVAVRVGNIDDRYFELARAEGHRVTNIAEAVAHADIVLllipdEAHGA--VFDVDIA 100
Cdd:smart00996 207 GKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMDGFEVVTMEEVAPQADIFV-----TTTGNkdVITREHM 281

                           90
                   ....*....|
7PCL_B         101 PNLRDGALLC 110
Cdd:smart00996 282 RAMKDGAIVC 291
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 18-82 5.29e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 38.63  E-value: 5.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7PCL_B        18 LQPLEGRTVAVIGYGIQGRAFAANLRDSGV-AVRVGNiddRYFE----LA---RAEGHRVTNIAEAVAHADIV 82
Cdd:PRK00045 177 FGDLSGKKVLVIGAGEMGELVAKHLAEKGVrKITVAN---RTLEraeeLAeefGGEAIPLDELPEALAEADIV 246
 
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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