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Conserved domains on  [gi|2324454601|gb|UYY93229|]
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alanine dehydrogenase [Bacillus cereus]

Protein Classification

alanine dehydrogenase( domain architecture ID 11430823)

alanine dehydrogenase catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate; alanine dehydrogenase catalyzes the reversible oxidative deamination of L-alanine to pyruvate

CATH:  3.40.50.720
EC:  1.4.1.1
Gene Ontology:  GO:0042853|GO:0000286
PubMed:  8226620|11888165
SCOP:  4000097

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 1-370 0e+00

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


:

Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 706.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQ-DMVMKVKEPVAS 79
Cdd:COG0686     1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIVDTAEEVFAQaDLIVKVKEPQPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  80 EYGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRSLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKGILL 159
Cdd:COG0686    81 EYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYETVEDPDGSLPLLAPMSEIAGRMAIQIGAEYLEKPNGGRGVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 160 AGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEAVKESDLVIGAVL 239
Cdd:COG0686   161 GGVPGVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDIFGGRVTTLYSNPANIEEALKEADLVIGAVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 240 IPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVP 319
Cdd:COG0686   241 IPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETS-RPTTHDDPTYVVHGVVHYCVANMPGAVPRTSTYALTNATLP 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2324454601 320 YAVQIANKGYKEACLGNTALLKGINTLDGYVTFEAVAEAHGLQYADAKELL 370
Cdd:COG0686   320 YLLALADKGWEQALREDPGLAKGLNTYKGKLTNKAVAEAFGLPYTDLELLL 370
 
Name Accession Description Interval E-value
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 1-370 0e+00

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 706.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQ-DMVMKVKEPVAS 79
Cdd:COG0686     1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIVDTAEEVFAQaDLIVKVKEPQPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  80 EYGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRSLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKGILL 159
Cdd:COG0686    81 EYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYETVEDPDGSLPLLAPMSEIAGRMAIQIGAEYLEKPNGGRGVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 160 AGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEAVKESDLVIGAVL 239
Cdd:COG0686   161 GGVPGVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDIFGGRVTTLYSNPANIEEALKEADLVIGAVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 240 IPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVP 319
Cdd:COG0686   241 IPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETS-RPTTHDDPTYVVHGVVHYCVANMPGAVPRTSTYALTNATLP 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2324454601 320 YAVQIANKGYKEACLGNTALLKGINTLDGYVTFEAVAEAHGLQYADAKELL 370
Cdd:COG0686   320 YLLALADKGWEQALREDPGLAKGLNTYKGKLTNKAVAEAFGLPYTDLELLL 370
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 1-359 0e+00

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 664.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQ-DMVMKVKEPVAS 79
Cdd:cd05305     1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIVPTAEEVWAKaDLIVKVKEPLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  80 EYGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRSLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKGILL 159
Cdd:cd05305    81 EYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYETIEDEDGSLPLLAPMSEIAGRLAVQIGAEYLEKPNGGRGVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 160 AGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEAVKESDLVIGAVL 239
Cdd:cd05305   161 GGVPGVPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTTLYSNPANLEEALKEADLVIGAVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 240 IPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVP 319
Cdd:cd05305   241 IPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETS-RPTTHDNPTYVVHGVIHYCVPNMPGAVPRTSTLALTNATLP 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2324454601 320 YAVQIANKGYKEACLGNTALLKGINTLDGYVTFEAVAEAH 359
Cdd:cd05305   320 YLLKLANKGLEEALLEDPGLAKGLNTYKGKLTNKAVAEAF 359
alaDH TIGR00518
alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes ...
 1-371 0e+00

alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes representatives from the Proteobacteria, Firmicutes, Cyanobacteria, and Actinobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homolog from Helicobacter pylori, an epsilon division Proteobacteria, which must be considered a putative alanine dehydrogenase. In Mycobacterium smegmatis and M. tuberculosis, the enzyme doubles as a glycine dehydrogenase (1.4.1.10), running in the reverse direction (glyoxylate amination to glycine, with conversion of NADH to NAD+). Related proteins include saccharopine dehydrogenase and the N-terminal half of the NAD(P) transhydrogenase alpha subunit. All of these related proteins bind NAD and/or NADP. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129609 [Multi-domain]  Cd Length: 370  Bit Score: 545.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQDMVMKVKEPVASE 80
Cdd:TIGR00518   1 MRIGVPKEIKNNEFRVALTPAGVAELTSRGHEVLVEAGAGEGSGFTDAAYKAAGAELVATAKQVWDAELVLKVKEPLPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  81 YGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRSLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKGILLA 160
Cdd:TIGR00518  81 YGYLRHGQILFTYLHLAAERALTDALLDSGTTAIAYETVQTADGALPLLAPMSEVAGRLAAQVGAYHLEKTQGGRGVLLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 161 GVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEAVKESDLVIGAVLI 240
Cdd:TIGR00518 161 GVPGVEPGDVTIIGGGVVGTNAAKMANGLGATVTILDINIDRLRQLDAEFGGRIHTRYSNAYEIEDAVKRADLLIGAVLI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 241 PGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVPY 320
Cdd:TIGR00518 241 PGAKAPKLVSNSLVAQMKPGAVIVDVAIDQGGCVETS-RPTTHDQPTYAVHDVVHYCVANMPGAVPKTSTYALTNATMPY 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2324454601 321 AVQIANKGYKEACLGNTALLKGINTLDGYVTFEAVAEAHGLQYADAKELLE 371
Cdd:TIGR00518 320 VLELANHGWRAACRSNPALAKGLNTHEGALLSEAVATDLGVPFTEPASVLA 370
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 140-352 3.41e-114

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 331.00  E-value: 3.41e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 140 SAQIGAQFLEKNKGGKGILLAGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQ-VKTLM 218
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVPGVAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESILGAKfVETLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 219 SNPYNIAEAVKESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAV 298
Cdd:pfam01262  81 SQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVETS-RPTTHGEPVYVVDGVVHYGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2324454601 299 ANMPGAVPRTSTLALTNVTVPYAVQIANKGYKEACLGNTALLKGINTLDGYVTF 352
Cdd:pfam01262 160 ANMPGAVPRTSSQALTNNTLPYLLLLADKGLKAALLEDEALRAGLNTHDGKITH 213
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 148-297 3.83e-77

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 234.32  E-value: 3.83e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  148 LEKNKGGKGILLAGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEA 227
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQAELLEEA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  228 VKESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYA 297
Cdd:smart01002  81 VKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETS-RPTTHDDPTYVVDGVVHYC 149
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-316 5.34e-54

Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 185.80  E-value: 5.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAeEAWNQDMVMKVKEPVASE 80
Cdd:PRK09424    1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGA-AVWQSDIILKVNAPSDDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  81 YGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNR--SLPLLAPMSEVAG------------RM-SAQIGA 145
Cdd:PRK09424   80 IALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRaqSLDALSSMANIAGyravieaahefgRFfTGQITA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 146 qfleknkGGKgillagvpgVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAErlrqlddiFGNQVKTL-------- 217
Cdd:PRK09424  160 -------AGK---------VPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPE--------VAEQVESMgaefleld 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 218 --------------MSNPYNIAEAV------KESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETT 277
Cdd:PRK09424  216 feeeggsgdgyakvMSEEFIKAEMAlfaeqaKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELT 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2324454601 278 --DRITTHDNptyekhGVVHYAVANMPGAVPR-TSTLALTNV 316
Cdd:PRK09424  296 vpGEVVVTDN------GVTIIGYTDLPSRLPTqSSQLYGTNL 331
 
Name Accession Description Interval E-value
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 1-370 0e+00

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 706.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQ-DMVMKVKEPVAS 79
Cdd:COG0686     1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIVDTAEEVFAQaDLIVKVKEPQPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  80 EYGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRSLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKGILL 159
Cdd:COG0686    81 EYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYETVEDPDGSLPLLAPMSEIAGRMAIQIGAEYLEKPNGGRGVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 160 AGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEAVKESDLVIGAVL 239
Cdd:COG0686   161 GGVPGVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDIFGGRVTTLYSNPANIEEALKEADLVIGAVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 240 IPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVP 319
Cdd:COG0686   241 IPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETS-RPTTHDDPTYVVHGVVHYCVANMPGAVPRTSTYALTNATLP 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2324454601 320 YAVQIANKGYKEACLGNTALLKGINTLDGYVTFEAVAEAHGLQYADAKELL 370
Cdd:COG0686   320 YLLALADKGWEQALREDPGLAKGLNTYKGKLTNKAVAEAFGLPYTDLELLL 370
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 1-359 0e+00

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 664.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQ-DMVMKVKEPVAS 79
Cdd:cd05305     1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIVPTAEEVWAKaDLIVKVKEPLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  80 EYGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRSLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKGILL 159
Cdd:cd05305    81 EYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYETIEDEDGSLPLLAPMSEIAGRLAVQIGAEYLEKPNGGRGVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 160 AGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEAVKESDLVIGAVL 239
Cdd:cd05305   161 GGVPGVPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTTLYSNPANLEEALKEADLVIGAVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 240 IPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVP 319
Cdd:cd05305   241 IPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETS-RPTTHDNPTYVVHGVIHYCVPNMPGAVPRTSTLALTNATLP 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2324454601 320 YAVQIANKGYKEACLGNTALLKGINTLDGYVTFEAVAEAH 359
Cdd:cd05305   320 YLLKLANKGLEEALLEDPGLAKGLNTYKGKLTNKAVAEAF 359
alaDH TIGR00518
alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes ...
 1-371 0e+00

alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes representatives from the Proteobacteria, Firmicutes, Cyanobacteria, and Actinobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homolog from Helicobacter pylori, an epsilon division Proteobacteria, which must be considered a putative alanine dehydrogenase. In Mycobacterium smegmatis and M. tuberculosis, the enzyme doubles as a glycine dehydrogenase (1.4.1.10), running in the reverse direction (glyoxylate amination to glycine, with conversion of NADH to NAD+). Related proteins include saccharopine dehydrogenase and the N-terminal half of the NAD(P) transhydrogenase alpha subunit. All of these related proteins bind NAD and/or NADP. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129609 [Multi-domain]  Cd Length: 370  Bit Score: 545.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQDMVMKVKEPVASE 80
Cdd:TIGR00518   1 MRIGVPKEIKNNEFRVALTPAGVAELTSRGHEVLVEAGAGEGSGFTDAAYKAAGAELVATAKQVWDAELVLKVKEPLPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  81 YGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRSLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKGILLA 160
Cdd:TIGR00518  81 YGYLRHGQILFTYLHLAAERALTDALLDSGTTAIAYETVQTADGALPLLAPMSEVAGRLAAQVGAYHLEKTQGGRGVLLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 161 GVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEAVKESDLVIGAVLI 240
Cdd:TIGR00518 161 GVPGVEPGDVTIIGGGVVGTNAAKMANGLGATVTILDINIDRLRQLDAEFGGRIHTRYSNAYEIEDAVKRADLLIGAVLI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 241 PGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVPY 320
Cdd:TIGR00518 241 PGAKAPKLVSNSLVAQMKPGAVIVDVAIDQGGCVETS-RPTTHDQPTYAVHDVVHYCVANMPGAVPKTSTYALTNATMPY 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2324454601 321 AVQIANKGYKEACLGNTALLKGINTLDGYVTFEAVAEAHGLQYADAKELLE 371
Cdd:TIGR00518 320 VLELANHGWRAACRSNPALAKGLNTHEGALLSEAVATDLGVPFTEPASVLA 370
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 140-352 3.41e-114

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 331.00  E-value: 3.41e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 140 SAQIGAQFLEKNKGGKGILLAGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQ-VKTLM 218
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVPGVAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESILGAKfVETLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 219 SNPYNIAEAVKESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAV 298
Cdd:pfam01262  81 SQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVETS-RPTTHGEPVYVVDGVVHYGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2324454601 299 ANMPGAVPRTSTLALTNVTVPYAVQIANKGYKEACLGNTALLKGINTLDGYVTF 352
Cdd:pfam01262 160 ANMPGAVPRTSSQALTNNTLPYLLLLADKGLKAALLEDEALRAGLNTHDGKITH 213
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 2-325 2.68e-113

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 332.84  E-value: 2.68e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   2 RIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETA-EEAWNQDMVMKVKEPVASE 80
Cdd:cd01620     1 TLGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIVPAAsKEAYSADIIVKLKEPEFAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  81 YGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNRslPLLAPMSEVAGRMSAQIGAQFLEKNKGGKgilLA 160
Cdd:cd01620    81 YDLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLENDFR--PRLAPNSNIAGYAGVQLGAYELARIQGGR---MG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 161 GVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTlmSNPYNIAEAVKESDLVIGAVLI 240
Cdd:cd01620   156 GAGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLRY--SQKEELEKELKQTDILINAILV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 241 PGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTSTLALTNVTVPY 320
Cdd:cd01620   234 DGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDETS-IPTTEGVPTYEVDGVVIYGVDNMPSLVPREASELLSKNLLPY 312


                  ....*
gi 2324454601 321 AVQIA 325
Cdd:cd01620   313 LVKLA 317
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 148-297 3.83e-77

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 234.32  E-value: 3.83e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  148 LEKNKGGKGILLAGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSNPYNIAEA 227
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQAELLEEA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  228 VKESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYA 297
Cdd:smart01002  81 VKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETS-RPTTHDDPTYVVDGVVHYC 149
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 4-136 2.78e-68

Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 461595 [Multi-domain]  Cd Length: 135  Bit Score: 211.13  E-value: 2.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   4 GIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQ-DMVMKVKEPVASEYG 82
Cdd:pfam05222   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIVDTAAEVWAEaDLILKVKEPQPEEYA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2324454601  83 YFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDN-RSLPLLAPMSEVA 136
Cdd:pfam05222  81 LLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPRSRgQSLDALSSMANIA 135
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 1-317 1.20e-65

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 212.27  E-value: 1.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQDMVMKVKEPVASE 80
Cdd:cd05304     1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELAQADIVLKVRPPSEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  81 YGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETV------QldnrSLPLLAPMSEVAGRMSAQIGAQFLEKnkgg 154
Cdd:cd05304    81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVprisraQ----SMDALSSQANIAGYKAVLEAANHLPR---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 155 kgillaGVPG-------VKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDL---SAErlrqlddifgnQVKTL------- 217
Cdd:cd05304   153 ------FFPMlmtaagtIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVrpaAKE-----------QVESLgakfvev 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 218 ---------------MSNPY------NIAEAVKESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFET 276
Cdd:cd05304   216 dveedaegaggyakeLSEEFlakqreLLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCEL 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2324454601 277 TDritthDNPTYEKHGVVHYAVANMPGAVPRT-STLALTNVT 317
Cdd:cd05304   296 TV-----PGETVVTNGVTIIGPTNLPSRLPTQaSQLYAKNLL 332
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-134 2.57e-62

Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214967 [Multi-domain]  Cd Length: 133  Bit Score: 196.10  E-value: 2.57e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601    4 GIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQDMVMKVKEPVASEYGY 83
Cdd:smart01003   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWADADIILKVKEPSPEELAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2324454601   84 FREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLD--NRSLPLLAPMSE 134
Cdd:smart01003  81 LREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRIsrAQSLDALSSMAE 133
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 3-322 1.37e-56

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: 187.44  E-value: 1.37e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   3 IGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQDMVMKVKEP-VASEY 81
Cdd:cd12154     1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVTLAKALWSLDVVLKVKEPlTNAEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  82 GYFREGLI--LFTYLHLAPEPELTKALIDNKVASIAYETVQldnrsLPLLAPMSEVAGRMSAQIGAQFLEKNKGGKgilL 159
Cdd:cd12154    81 ALIQKLGDrlLFTYTIGADHRDLTEALARAGLTAIAVEGVE-----LPLLTSNSIGAGELSVQFIARFLEVQQPGR---L 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 160 AGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMsnpyniaEAVKESDLVIGAVL 239
Cdd:cd12154   153 GGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVEELE-------EALAEADVIVTTTL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 240 IPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGifettDRITTHDNPTYEKHGVVHYAVANMPGA-----VPRTSTLALT 314
Cdd:cd12154   226 LPGKRAGILVPEELVEQMKPGSVIVNVAVGAVG-----CVQALHTQLLEEGHGVVHYGDVNMPGPgcamgVPWDATLRLA 300


                  ....*...
gi 2324454601 315 NVTVPYAV 322
Cdd:cd12154   301 ANTLPALV 308
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-316 5.34e-54

Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 185.80  E-value: 5.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAeEAWNQDMVMKVKEPVASE 80
Cdd:PRK09424    1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGA-AVWQSDIILKVNAPSDDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  81 YGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNR--SLPLLAPMSEVAG------------RM-SAQIGA 145
Cdd:PRK09424   80 IALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRaqSLDALSSMANIAGyravieaahefgRFfTGQITA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 146 qfleknkGGKgillagvpgVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAErlrqlddiFGNQVKTL-------- 217
Cdd:PRK09424  160 -------AGK---------VPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPE--------VAEQVESMgaefleld 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 218 --------------MSNPYNIAEAV------KESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFETT 277
Cdd:PRK09424  216 feeeggsgdgyakvMSEEFIKAEMAlfaeqaKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELT 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2324454601 278 --DRITTHDNptyekhGVVHYAVANMPGAVPR-TSTLALTNV 316
Cdd:PRK09424  296 vpGEVVVTDN------GVTIIGYTDLPSRLPTqSSQLYGTNL 331
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
1-317 1.50e-53

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 180.97  E-value: 1.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVetAEEAWNQDMVMKVKEPVASE 80
Cdd:COG3288     1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIV--DAELLGADIVLKVRPPSAEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  81 YGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETVQLDNR--SLPLLAPMSEVAGRMSAQIGAQFLeknkgGKGI- 157
Cdd:COG3288    79 LAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRaqSMDALSSQANFAGYKAVLLAAPAL-----HTFFp 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 158 LLAGVPG-VKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQ-------------LDDIFGNQVKTLMSNPYN 223
Cdd:COG3288   154 LMSTAAGtIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQveslgakfvelaiDANGAGGYAKELSEEEKA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 224 -----IAEAVKESDLVIGAVLIPGAKAPKLVTEEMIQSMEPGSVVVDIAIDQGGIFEttdriTTHDNPTYEKHGVVHYAV 298
Cdd:COG3288   234 kqaelLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCE-----LTVPGETVTKNGVTIIGP 308

                         330       340
                  ....*....|....*....|
gi 2324454601 299 ANMPGAVPRT-STLALTNVT 317
Cdd:COG3288   309 TNLPSRLPAHaSQLYAKNLL 328
ceo_syn cd12181
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ...
 1-320 8.36e-43

N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) catalyzes the NADP-dependent conversion of N5-(L-1-carboxyethyl)-L-ornithine to L-ornithine + pyruvate. Ornithine plays a key role in the urea cycle, which in mammals is used in arginine biosynthesis, and is a precursor in polyamine synthesis. ceo_syn is related to the NAD-dependent L-alanine dehydrogenases. Like formate dehydrogenase and related enzymes, ceo_syn is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. These ceo_syn proteins have a partially conserved NAD-binding motif and active site residues that are characteristic of related enzymes such as Saccharopine Dehydrogenase.


Pssm-ID: 240658 [Multi-domain]  Cd Length: 295  Bit Score: 150.84  E-value: 8.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   1 MRIGIPTEIKNNENRVAMTPAgavHL--VQNGHEVFVQKGAGLGSGFTDEEYVQAGAKLVETAEEAWNQDMVMKVKePVA 78
Cdd:cd12181     1 KTGGFGISNKENEKRVPLLPA---DLerIPLREQLYFEEGYGERLGISDEEYAALGAGIVSREEILAKCDVICDPK-PGD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  79 SEYGYFREGLILFTYLHLAPEPELTKALIDNKVASIAYETvqldnrslpllapMSEvagrmSAQIGAQFLEKNK---GGK 155
Cdd:cd12181    77 ADYLEILEGQILWGWVHCVQDKEITQLAIDKKLTLIAWED-------------MFE-----WSKIGRHVFYKNNelaGYA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 156 GIL----LAGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAErlrqlddifgNQVKTLMSnpyniaeavkES 231
Cdd:cd12181   139 AVLhalqLYGITPYRQTKVAVLGFGNTARGAIRALKLGGADVTVYTRRTE----------ALFKEELS----------EY 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 232 DLVIGAVLIpGAKAPK-LVTEEMIQSMEPGSVVVDIAIDQGGIFETTdRITTHDNPTYEKHGVVHYAVANMPGAVPRTST 310
Cdd:cd12181   199 DIIVNCILQ-DTDRPDhIIYEEDLKRLKPGALIIDVSCDEGMGIEFA-KPTTFDDPIYKVDGIDYYAVDHTPSLFYRSAS 276

                         330
                  ....*....|
gi 2324454601 311 LALTNVTVPY 320
Cdd:cd12181   277 RSISKALAPY 286
SDH_like cd05199
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ...
 3-320 6.13e-15

Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related proteins, including bifunctional lysine ketoglutarate reductase/SDH enzymes and N(5)-(carboxyethyl)ornithine synthases. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SDH is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure. Bifunctional lysine ketoglutarate reductase/SDH protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases.


Pssm-ID: 240623 [Multi-domain]  Cd Length: 319  Bit Score: 74.96  E-value: 6.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   3 IGIPTEIKNN-ENRVAMTPAGAVHLVQNGH--EVFVQKGAGlgSGFTDEEYVQAGAKLVETAEEAwnqDMVMKVKE-PVA 78
Cdd:cd05199     2 IGIIREGKTPpDRRVPLTPEQCKELQAKYPgvEIFVQPSPV--RCFKDEEYRAAGIEVVEDLSDC---DILLGVKEvPIE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  79 SeygyfregLIL-FTYL---HLAPEPE----LTKALIDNKVASIAYEtVQLDNRSLPLLApmsevAGRMSAQIGA----- 145
Cdd:cd05199    77 Q--------LIPnKTYFffsHTIKKQPynrkLLQTILEKNITLIDYE-VLVDEQGKRVIA-----FGRYAGIVGAynglr 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 146 ---------------QFLEKNKGGKGILLAGVPGVkrgKVTIIGGGQAGTNAAKIAVGLGA-DVTIIDLsaerLRQLDdi 209
Cdd:cd05199   143 aygkktglfdlkrahECSDLEELIAELKKVGLPPP---KIVITGSGRVGSGAAEVLKALGIkEVSPEDF----LTVAD-- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 210 fgnqvktlmsnpyniaeavkesdlvigaVLIPGA----KAPKLVTEEMIQSME-PGSVVVDIAIDQGGIFETTDRITTHD 284
Cdd:cd05199   214 ----------------------------ILINGHywdkRAPRLFTKEDLKKPDfKIRVIADVTCDIHGSIPSTLRASTIA 265

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2324454601 285 NPTY-------------EKHGVVHYAVANMPGAVPRTSTLALTNVTVPY 320
Cdd:cd05199   266 DPVYdydpttnkevafsSPDSITVMAVDNLPCELPRDASEDFGEQLIKS 314
SDH cd12188
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ...
 8-326 5.60e-14

Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure.


Pssm-ID: 240664 [Multi-domain]  Cd Length: 351  Bit Score: 72.26  E-value: 5.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601   8 EIKNNENRVAMTPAGAVHLVQNGHEVFVQKGAglGSGFTDEEYVQAGAKLVEtaEEAW----NQDMVMKVKE------PV 77
Cdd:cd12188     8 ETKPLERRTALTPTTAKKLLDAGFKVTVERSP--QRIFPDEEYEAVGCELVP--AGSWvnapKDAIILGLKElpedtfPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  78 ASEYGYF----------REGLILF-----TYLHLapepeltKALIDNK-----------------VASIAYETVQLDNRS 125
Cdd:cd12188    84 PHRHIYFahaykgqagwKDVLSRFargggTLLDL-------EYLVDDDgrrvaafgywagfagaaLGLLAWAHQQLGPVT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 126 LPLLAPMSevagrmSAQIGAQFLEKNKGGKGillagvpgvKRGKVTIIG-GGQAGTNAAKIAVGLGADVTIIDLsAErlr 204
Cdd:cd12188   157 LPPVSPYP------NEEALVADVKKALATGG---------RKPRALVIGaLGRCGSGAVDLLEAAGIEVTKWDM-AE--- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 205 qlddifgnqvkTLMSNPYNiaeAVKESDLVIGAVLIPGaKAPKLVTEEMIQSmePG---SVVVDIAIDQGG------IFe 275
Cdd:cd12188   218 -----------TKAGGPFP---EILDHDIFVNCIYLSK-PIPPFLTPEMLQA--PGrrlRVIGDVSCDPTNpynpipIY- 279

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2324454601 276 ttDRITTHDNPTYEKHG------VVhyAVANMPGAVPRTSTLALTNVTVPYAVQIAN 326
Cdd:cd12188   280 --DVATTFDKPTLRVPTggppldVI--AIDHLPSLLPRESSEDFSNDLLPSLLELAE 332
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
 169-285 2.91e-06

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 48.59  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKI-AVGLGADVTIIdlsaerlrqldDIFGNQ-VKTLMSNPYNIAEAVKESDLVigAVLIPGAKA- 245
Cdd:PRK08605  148 KVAVIGTGRIGLAVAKIfAKGYGSDVVAY-----------DPFPNAkAATYVDYKDTIEEAVEGADIV--TLHMPATKYn 214

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2324454601 246 PKLVTEEMIQSMEPGSVVVDIAidQGGIFETTDRITTHDN 285
Cdd:PRK08605  215 HYLFNADLFKHFKKGAVFVNCA--RGSLVDTKALLDALDN 252
LKR_SDH_like cd12189
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ...
 3-76 3.58e-06

bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.


Pssm-ID: 240665 [Multi-domain]  Cd Length: 433  Bit Score: 48.71  E-value: 3.58e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2324454601   3 IGIPTEIKNN-ENRVAMTPAGAVHLVQN-GHEVFVQKgaglgSG---FTDEEYVQAGAKLVETAEEAwnqDMVMKVKEP 76
Cdd:cd12189     2 IGIRREDKNIwERRAPLTPSHVRELVKKpGVKVLVQP-----SNrraFPDQEYEAAGAIIQEDLSDA---DLILGVKEP 72
trkA PRK09496
Trk system potassium transporter TrkA;
169-238 4.99e-06

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 48.19  E-value: 4.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDD------IFGN--QVKTLMsnpyniaEA-VKESDLVIgAV 238
Cdd:PRK09496    2 KIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDrldvrtVVGNgsSPDVLR-------EAgAEDADLLI-AV 72
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 162-268 5.23e-05

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 42.56  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 162 VPGVKRGKVTIIGGGQAGTNAAKIAVGLGA-DVTIIDLSAERLRQLDDIFGNQVKTLMSnpyNIAEAVKESDLVIGAVli 240
Cdd:pfam01488   7 FGDLKDKKVLLIGAGEMGELVAKHLLAKGAkEVTIANRTIERAQELAEKFGGVEALPLD---DLKEYLAEADIVISAT-- 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2324454601 241 pGAKAPkLVTEEMIQSMEPGS----VVVDIAI 268
Cdd:pfam01488  82 -SSPTP-IITKEMVERALKPRkkplLFVDIAV 111
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
168-266 1.26e-04

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 43.42  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 168 GKVTIIGGGQAGTNAAKIA--VGLGADVTIIDLSAERLRQLDDI-FGNQVKTlmsnpyNIAEAVKESDLVIGAVLIpGAK 244
Cdd:PRK07502    7 DRVALIGIGLIGSSLARAIrrLGLAGEIVGADRSAETRARARELgLGDRVTT------SAAEAVKGADLVILCVPV-GAS 79

                          90       100
                  ....*....|....*....|..
gi 2324454601 245 APklVTEEMIQSMEPGSVVVDI 266
Cdd:PRK07502   80 GA--VAAEIAPHLKPGAIVTDV 99
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
 169-263 1.37e-04

NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133453 [Multi-domain]  Cd Length: 226  Bit Score: 42.64  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGAD---VTIID----LSAERLRQLDDIFgNQVKTLmSNPYN----IAEAVKESDLVIga 237
Cdd:cd05311    27 KIVINGAGAAGIAIARLLLAAGAKpenIVVVDskgvIYEGREDDLNPDK-NEIAKE-TNPEKtggtLKEALKGADVFI-- 102

                          90       100
                  ....*....|....*....|....*.
gi 2324454601 238 vlipGAKAPKLVTEEMIQSMEPGSVV 263
Cdd:cd05311   103 ----GVSRPGVVKKEMIKKMAKDPIV 124
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 169-268 1.62e-04

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 43.56  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGA-DVTIIDLSAERLRQLDDIFGNQVKTLMsnpyNIAEAVKESDLVIGAVlipGAKAPk 247
Cdd:COG0373   184 TVLVIGAGEMGELAARHLAAKGVkRITVANRTLERAEELAEEFGGEAVPLE----ELPEALAEADIVISST---GAPHP- 255

                          90       100
                  ....*....|....*....|....*.
gi 2324454601 248 LVTEEMIQSMEPGS-----VVVDIAI 268
Cdd:COG0373   256 VITKEMVERALKKRrhrplFLIDLAV 281
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
 165-267 1.95e-04

(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic domains; (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. HGDH is a member of the D-2-hydroxyacid NAD(+)-dependent dehydrogenase family; 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.


Pssm-ID: 240660  Cd Length: 330  Bit Score: 43.05  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 165 VKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERlrqlddiFGNQVKTLMSNPyniaEAVKESDLV-IGAVLIPGa 243
Cdd:cd12184   143 IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSD-------AAKDVVTFVSLD----ELLKKSDIIsLHVPYIKG- 210

                          90       100
                  ....*....|....*....|....
gi 2324454601 244 KAPKLVTEEMIQSMEPGSVVVDIA 267
Cdd:cd12184   211 KNDKLINKEFISKMKDGAILINTA 234
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
170-282 2.27e-04

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 42.08  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 170 VTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTlMSNpyniAEAVKESDLVIGAVliPGAKAPKLV 249
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGARA-GTN----AEAAAAADVVVLAV--PYEAVPDVL 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2324454601 250 teEMIQSMEPGSVVVDIA----IDQGGIFETTDRITT 282
Cdd:COG2085    74 --ESLGDALAGKIVIDATnplpERDGFILDPPGGGSA 108
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 166-208 2.47e-04

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 42.36  E-value: 2.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2324454601 166 KRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDD 208
Cdd:COG0569    94 LKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAE 136
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
169-238 3.74e-04

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 41.85  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAE-------RLRQLDDIFGNQVKTLMSNP-----------YNIAEAVKE 230
Cdd:PRK08293    5 NVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEalekakeRIAKLADRYVRDLEATKEAPaeaalnritltTDLAEAVKD 84


                  ....*...
gi 2324454601 231 SDLVIGAV 238
Cdd:PRK08293   85 ADLVIEAV 92
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 169-197 5.02e-04

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 41.77  E-value: 5.02e-04
                          10        20
                  ....*....|....*....|....*....
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGADVTIID 197
Cdd:PRK07845    3 RIVIIGGGPGGYEAALVAAQLGADVTVIE 31
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 169-220 5.18e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 38.34  E-value: 5.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSN 220
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEK 52
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
 165-287 6.39e-04

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 41.44  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 165 VKRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLsaerlrqlddiFGNQVKTLMSNPYNIAEAVKESDLVigAVLIPGAK 244
Cdd:PRK12480  144 VKNMTVAIIGTGRIGAATAKIYAGFGATITAYDA-----------YPNKDLDFLTYKDSVKEAIKDADII--SLHVPANK 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2324454601 245 AP-KLVTEEMIQSMEPGSVVVDIAidQGGIFETTDRITTHDNPT 287
Cdd:PRK12480  211 ESyHLFDKAMFDHVKKGAILVNAA--RGAVINTPDLIAAVNDGT 252
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 166-220 7.10e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 41.15  E-value: 7.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2324454601 166 KRGKVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVKTLMSN 220
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEK 205
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
166-267 7.57e-04

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 40.98  E-value: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 166 KRGKVTIIGG-GQAGTNAAKIAVGLGADVTIIDLSAERLRQL-DDIFGN---QVKTLMsnpyNIAEAVKESDLVIGAvli 240
Cdd:COG5322   150 KKATVAVVGAtGSIGSVCARLLAREVKRLTLVARNLERLEELaEEILRNpggKVTITT----DIDEALREADIVVTV--- 222

                          90       100
                  ....*....|....*....|....*..
gi 2324454601 241 pgAKAPKLVTEemIQSMEPGSVVVDIA 267
Cdd:COG5322   223 --TSAVGAIID--PEDLKPGAVVCDVA 245
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 167-275 7.82e-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: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 41.07  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 167 RGK-VTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQvktlmsnpyNIAEAVKESDLVIgaVLIPGAKA 245
Cdd:cd12165   136 RGKtVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGTLS---------DLDEALEQADVVV--VALPLTKQ 204

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2324454601 246 PK-LVTEEMIQSMEPGSVVVDIA----IDQGGIFE 275
Cdd:cd12165   205 TRgLIGAAELAAMKPGAILVNVGrgpvVDEEALYE 239
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
223-272 8.68e-04

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;


Pssm-ID: 427036  Cd Length: 160  Bit Score: 39.37  E-value: 8.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2324454601 223 NIAEAVKESDLVIGAVLIPGakapkLVTEEMIQsmePGSVVVDIAIDQGG 272
Cdd:pfam02882  72 DLAEITREADIVVVAVGKPE-----LIKADWIK---PGAVVIDVGINRVG 113
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 161-204 8.74e-04

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 41.02  E-value: 8.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2324454601 161 GVPGVKRGKVT------IIGGGQAGTNAAKIAVGLGADVTIIDLSAERLR 204
Cdd:cd08261   148 GAHAVRRAGVTagdtvlVVGAGPIGLGVIQVAKARGARVIVVDIDDERLE 197
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 169-267 1.00e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 40.94  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGA-DVTIIDLSAERLRQLDDIFGNQVKTLmsnpYNIAEAVKESDLVIGAVlipGAKAPk 247
Cdd:PRK00045  184 KVLVIGAGEMGELVAKHLAEKGVrKITVANRTLERAEELAEEFGGEAIPL----DELPEALAEADIVISST---GAPHP- 255

                          90       100
                  ....*....|....*....|....*
gi 2324454601 248 LVTEEMIQSMEPGS-----VVVDIA 267
Cdd:PRK00045  256 IIGKGMVERALKARrhrplLLVDLA 280
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
172-267 1.05e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 37.98  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 172 IIGGGQAGTNAAKIAVGLGA-DVTII-DLSAERLRQLDDIFGNQVKTlMSNpyniAEAVKESDLVIGAVliPGAKAPKLV 249
Cdd:pfam03807   2 FIGAGNMGEALARGLVAAGPhEVVVAnSRNPEKAEELAEEYGVGATA-VDN----EEAAEEADVVFLAV--KPEDAPDVL 74

                          90
                  ....*....|....*...
gi 2324454601 250 TEemIQSMEPGSVVVDIA 267
Cdd:pfam03807  75 SE--LSDLLKGKIVISIA 90
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 167-267 1.21e-03

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: 39.40  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 167 RGK-VTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERLRQLDDIFGNQVktlmsnpyNIAEAVKESDLVIgaVLIPGAKA 245
Cdd:pfam02826  35 SGKtVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYV--------SLDELLAESDVVS--LHLPLTPE 104

                          90       100
                  ....*....|....*....|...
gi 2324454601 246 PK-LVTEEMIQSMEPGSVVVDIA 267
Cdd:pfam02826 105 TRhLINAERLALMKPGAILINTA 127
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 169-267 1.29e-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: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNaakIAVGL------GADVTIIDLSAERLRQLDDIFGnqVKTLMSNpyniAEAVKESDLVIGAVlipg 242
Cdd:COG0345     4 KIGFIGAGNMGSA---IIKGLlksgvpPEDIIVSDRSPERLEALAERYG--VRVTTDN----AEAAAQADVVVLAV---- 70

                          90       100
                  ....*....|....*....|....*...
gi 2324454601 243 aKaPKL---VTEEMIQSMEPGSVVVDIA 267
Cdd:COG0345    71 -K-PQDlaeVLEELAPLLDPDKLVISIA 96
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 213-269 1.32e-03

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.


Pssm-ID: 133448  Cd Length: 168  Bit Score: 39.08  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2324454601 213 QVKTLMSNPYNIAEAVKESDLVIGAVLIPGakapkLVTEEMIQsmePGSVVVDIAID 269
Cdd:cd01080    70 TVTVCHSKTKNLKEHTKQADIVIVAVGKPG-----LVKGDMVK---PGAVVIDVGIN 118
LKR_SDH_like cd12189
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ...
 238-325 1.65e-03

bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.


Pssm-ID: 240665 [Multi-domain]  Cd Length: 433  Bit Score: 40.23  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 238 VLIPG----AKAPKLVT-EEMIQSMEPGS------VVVDIAIDQGGIFETTDRITTHDNPTY-------------EKHGV 293
Cdd:cd12189   283 VLINGiywdPRFPRLLTnEQLQALLRPPAgphrllAIADISCDIGGSIEFLTKATTIDSPFYvydpdtdkihdsvSGDGI 362

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2324454601 294 VHYAVANMPGAVPRTSTLALTNVTVPYAVQIA 325
Cdd:cd12189   363 LVMSVDNLPAELPREASEHFGDALLPYVPDLA 394
PRK08306 PRK08306
dipicolinate synthase subunit DpsA;
169-275 2.43e-03

dipicolinate synthase subunit DpsA;


Pssm-ID: 181371 [Multi-domain]  Cd Length: 296  Bit Score: 39.44  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGADVTIidlSAERLRQLDDIFGNQVKTLMSNpyNIAEAVKESDLVIGAVlipgakaPKL 248
Cdd:PRK08306  154 NVLVLGFGRTGMTLARTLKALGANVTV---GARKSAHLARITEMGLSPFHLS--ELAEEVGKIDIIFNTI-------PAL 221

                          90       100
                  ....*....|....*....|....*....
gi 2324454601 249 V-TEEMIQSMEPGSVVVDIAIDQGGI-FE 275
Cdd:PRK08306  222 VlTKEVLSKMPPEALIIDLASKPGGTdFE 250
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
 169-263 2.58e-03

Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.


Pssm-ID: 214912  Cd Length: 231  Bit Score: 38.93  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601  169 KVTIIGGGQAGTNAAKIAVGLGA---DVTIID----LSAERLRQLDDIfgnQ----VKTLMSNPYNIAEAVKESDLVIGA 237
Cdd:smart00919  27 RIVVNGAGAAGIGIAKLLVAAGVkrkNIWLVDskglLTKGREDNLNPY---KkpfaRKTNERETGTLEEAVKGADVLIGV 103

                           90       100
                   ....*....|....*....|....*.
gi 2324454601  238 vlipgAKAPKLVTEEMIQSMEPGSVV 263
Cdd:smart00919 104 -----SGPGGAFTEEMVKSMAERPII 124
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 170-197 2.69e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 39.68  E-value: 2.69e-03
                          10        20
                  ....*....|....*....|....*...
gi 2324454601 170 VTIIGGGQAGTNAAKIAVGLGADVTIID 197
Cdd:COG1249     6 LVVIGAGPGGYVAAIRAAQLGLKVALVE 33
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 169-280 4.59e-03

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. 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.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 38.67  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGADVTIIDLsaERLRQLDDIFGNQVktlmsnpyNIAEAVKESDLVigAVLIPGAKAPK- 247
Cdd:cd12186   147 TVGIIGTGRIGSAAAKIFKGFGAKVIAYDP--YPNPELEKFLLYYD--------SLEDLLKQADII--SLHVPLTKENHh 214

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2324454601 248 LVTEEMIQSMEPGSVVVDIAidQGGIFETTDRI 280
Cdd:cd12186   215 LINAEAFAKMKDGAILVNAA--RGGLVDTKALI 245
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 158-267 6.64e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 36.87  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454601 158 LLAGVPGVKRGKVTIIGGGQAGTNAAKIAVGLGA-DVTIIDLSAERLRQLDDIFGNQVKTLMSnpYNIAEAVKESDLVIG 236
Cdd:cd01065    10 LEEAGIELKGKKVLILGAGGAARAVAYALAELGAaKIVIVNRTLEKAKALAERFGELGIAIAY--LDLEELLAEADLIIN 87

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2324454601 237 AvlIPGAKAPKLVTEEMIQSMEPGSVVVDIA 267
Cdd:cd01065    88 T--TPVGMKPGDELPLPPSLLKPGGVVYDVV 116
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 164-203 9.71e-03

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 37.78  E-value: 9.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2324454601 164 GVKRG-KVTIIGGGQAGTNAAKIAVGLGADVTIIDLSAERL 203
Cdd:COG1064   159 GVGPGdRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKL 199
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 169-198 1.00e-02

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 37.68  E-value: 1.00e-02
                          10        20        30
                  ....*....|....*....|....*....|
gi 2324454601 169 KVTIIGGGQAGTNAAKIAVGLGADVTIIDL 198
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIED 31
 
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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