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Conserved domains on  [gi|505960963|ref|WP_015728942|]
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5-(carboxyamino)imidazole ribonucleotide synthase [Staphylococcus pseudintermedius]

Protein Classification

5-(carboxyamino)imidazole ribonucleotide synthase( domain architecture ID 11481947)

5-(carboxyamino)imidazole ribonucleotide synthase catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR)

Gene Ontology:  GO:0005524|GO:0034028|GO:0046872
PubMed:  10569930

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 9-366 0e+00

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


:

Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 519.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQT 88
Cdd:PRK06019   2 MKTIGIIGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQCDVITYEFENVPAEALDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  89 LVSKYNVPQSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQL 168
Cdd:PRK06019  82 LAARVPVPPGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRGGYDGKGQWVIRSAEDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 169 DEARELIANQECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPARANHE--QEARREVDKITQAVH 246
Cdd:PRK06019 162 EAAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVENVHRNGILRTSIAPARISAElqAQAEEIASRIAEELD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 247 FVGTFTVEFFIDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEhIELLKPAIMMNLLGKD-LDLLEK 325
Cdd:PRK06019 242 YVGVLAVEFFVTGDGELLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLGT-TRLLSPAVMVNLLGDDwLEPRWD 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 505960963 326 ELFAHPDWHVHLYGKVSRKPERKMGHLTILTDDVSKTEQQL 366
Cdd:PRK06019 321 ALLALPGAHLHLYGKAEARPGRKMGHVTVLGDDVEALLAKL 361
 
Name Accession Description Interval E-value
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 9-366 0e+00

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 519.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQT 88
Cdd:PRK06019   2 MKTIGIIGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQCDVITYEFENVPAEALDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  89 LVSKYNVPQSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQL 168
Cdd:PRK06019  82 LAARVPVPPGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRGGYDGKGQWVIRSAEDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 169 DEARELIANQECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPARANHE--QEARREVDKITQAVH 246
Cdd:PRK06019 162 EAAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVENVHRNGILRTSIAPARISAElqAQAEEIASRIAEELD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 247 FVGTFTVEFFIDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEhIELLKPAIMMNLLGKD-LDLLEK 325
Cdd:PRK06019 242 YVGVLAVEFFVTGDGELLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLGT-TRLLSPAVMVNLLGDDwLEPRWD 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 505960963 326 ELFAHPDWHVHLYGKVSRKPERKMGHLTILTDDVSKTEQQL 366
Cdd:PRK06019 321 ALLALPGAHLHLYGKAEARPGRKMGHVTVLGDDVEALLAKL 361
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 19-366 2.36e-172

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 484.19  E-value: 2.36e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  19 QLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQTLVSKYNVPQS 98
Cdd:COG0026    1 QLGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREFAERCDVVTFEFENVPAEALEALEAEVPVRPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  99 YQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQLDEARELIANQ 178
Cdd:COG0026   81 PEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRGGYDGKGQVVIKSAADLEAAWAALGGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 179 ECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPARANHE--QEARREVDKITQAVHFVGTFTVEFF 256
Cdd:COG0026  161 PCILEEFVPFERELSVIVARSPDGEVATYPVVENVHRNGILDESIAPARISEAlaAEAEEIAKRIAEALDYVGVLAVEFF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 257 IDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEhIELLKPAIMMNLLGKDL-DLLEKELFAHPDWHV 335
Cdd:COG0026  241 VTKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGD-TELLSPAVMVNLLGDDWeDPGWEALLALPGAHL 319

                        330       340       350
                 ....*....|....*....|....*....|.
gi 505960963 336 HLYGKVSRKPERKMGHLTILTDDVSKTEQQL 366
Cdd:COG0026  320 HLYGKKEARPGRKMGHVTVLGDDLEEALERA 350
purK TIGR01161
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ...
 11-358 1.26e-121

phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273473 [Multi-domain]  Cd Length: 352  Bit Score: 355.49  E-value: 1.26e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   11 TVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQTLV 90
Cdd:TIGR01161   1 TVGILGGGQLGRMLALAARPLGIKVHVLDPDANSPAVQVADHVVLAPFFDPAAIRELAESCDVITFEFEHVDVEALEKLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   91 -SKYNVPQSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQLD 169
Cdd:TIGR01161  81 aRGVKLFPSPDALAIIQDRLTQKQFLQKLGLPVPPFLVIKDEEELDAALQELGFPVVLKARTGGYDGRGQYRIRNEADLP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  170 EARELIANQECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPAR--ANHEQEARREVDKITQAVHF 247
Cdd:TIGR01161 161 QAAKELGDRECIVEEFVPFERELSVIVARSADGETAFYPVVENIHQDGILRYVVAPAAvpDAIQARAEEIARRLMEELGY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  248 VGTFTVEFFIDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEhIELLKPAIMMNLLGKDLD--LLEK 325
Cdd:TIGR01161 241 VGVLAVEMFVLPDGRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGS-TELLLPSVMVNLLGTEDDviPLWE 319

                         330       340       350
                  ....*....|....*....|....*....|...
gi 505960963  326 ELFAHPDWHVHLYGKVSRKPERKMGHLTILTDD 358
Cdd:TIGR01161 320 EILALPGAKLHWYGKAEVRPGRKVGHVNLVGSD 352
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 116-282 2.08e-49

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 163.96  E-value: 2.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  116 AQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQLDEARELIANQECVAEQFLDLAKEVSLT 195
Cdd:pfam02222   1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGYDGKGQYVVRSEADLPQAWEELGDGPVIVEEFVPFDRELSVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  196 VTIGNEGQMVYFPLQENEHRNQVLFKTVVPARANHEQEARRE--VDKITQAVHFVGTFTVEFFIDQQNELYVNEIAPRPH 273
Cdd:pfam02222  81 VVRSVDGETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQdiAKRLVDELGGVGVFGVELFVTEDGDLLINELAPRPH 160


                  ....*....
gi 505960963  274 NSGHYSIEA 282
Cdd:pfam02222 161 NSGHYTLDG 169
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 9-75 7.15e-07

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 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. 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. 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 hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. 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, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 50.32  E-value: 7.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDpdetcpcRYVAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd05198  140 GKTVGIVGLGRIGQRVAKRLQAFGMKVLYYD-------RTRKPEPEEDLGFRVVSLDELLAQSDVVV 199
 
Name Accession Description Interval E-value
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 9-366 0e+00

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 519.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQT 88
Cdd:PRK06019   2 MKTIGIIGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQCDVITYEFENVPAEALDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  89 LVSKYNVPQSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQL 168
Cdd:PRK06019  82 LAARVPVPPGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRGGYDGKGQWVIRSAEDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 169 DEARELIANQECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPARANHE--QEARREVDKITQAVH 246
Cdd:PRK06019 162 EAAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVENVHRNGILRTSIAPARISAElqAQAEEIASRIAEELD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 247 FVGTFTVEFFIDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEhIELLKPAIMMNLLGKD-LDLLEK 325
Cdd:PRK06019 242 YVGVLAVEFFVTGDGELLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLGT-TRLLSPAVMVNLLGDDwLEPRWD 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 505960963 326 ELFAHPDWHVHLYGKVSRKPERKMGHLTILTDDVSKTEQQL 366
Cdd:PRK06019 321 ALLALPGAHLHLYGKAEARPGRKMGHVTVLGDDVEALLAKL 361
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 19-366 2.36e-172

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 484.19  E-value: 2.36e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  19 QLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQTLVSKYNVPQS 98
Cdd:COG0026    1 QLGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREFAERCDVVTFEFENVPAEALEALEAEVPVRPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  99 YQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQLDEARELIANQ 178
Cdd:COG0026   81 PEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRGGYDGKGQVVIKSAADLEAAWAALGGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 179 ECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPARANHE--QEARREVDKITQAVHFVGTFTVEFF 256
Cdd:COG0026  161 PCILEEFVPFERELSVIVARSPDGEVATYPVVENVHRNGILDESIAPARISEAlaAEAEEIAKRIAEALDYVGVLAVEFF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 257 IDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEhIELLKPAIMMNLLGKDL-DLLEKELFAHPDWHV 335
Cdd:COG0026  241 VTKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGD-TELLSPAVMVNLLGDDWeDPGWEALLALPGAHL 319

                        330       340       350
                 ....*....|....*....|....*....|.
gi 505960963 336 HLYGKVSRKPERKMGHLTILTDDVSKTEQQL 366
Cdd:COG0026  320 HLYGKKEARPGRKMGHVTVLGDDLEEALERA 350
purK TIGR01161
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ...
 11-358 1.26e-121

phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273473 [Multi-domain]  Cd Length: 352  Bit Score: 355.49  E-value: 1.26e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   11 TVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQTLV 90
Cdd:TIGR01161   1 TVGILGGGQLGRMLALAARPLGIKVHVLDPDANSPAVQVADHVVLAPFFDPAAIRELAESCDVITFEFEHVDVEALEKLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   91 -SKYNVPQSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQLD 169
Cdd:TIGR01161  81 aRGVKLFPSPDALAIIQDRLTQKQFLQKLGLPVPPFLVIKDEEELDAALQELGFPVVLKARTGGYDGRGQYRIRNEADLP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  170 EARELIANQECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPAR--ANHEQEARREVDKITQAVHF 247
Cdd:TIGR01161 161 QAAKELGDRECIVEEFVPFERELSVIVARSADGETAFYPVVENIHQDGILRYVVAPAAvpDAIQARAEEIARRLMEELGY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  248 VGTFTVEFFIDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEhIELLKPAIMMNLLGKDLD--LLEK 325
Cdd:TIGR01161 241 VGVLAVEMFVLPDGRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGS-TELLLPSVMVNLLGTEDDviPLWE 319

                         330       340       350
                  ....*....|....*....|....*....|...
gi 505960963  326 ELFAHPDWHVHLYGKVSRKPERKMGHLTILTDD 358
Cdd:TIGR01161 320 EILALPGAKLHWYGKAEVRPGRKVGHVNLVGSD 352
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
 12-376 1.14e-85

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 270.78  E-value: 1.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  12 VGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEFIHAAYDDMPALERLGERSDVITYEFENIAAEQLQTLVS 91
Cdd:PLN02948  25 VGVLGGGQLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGSFDDRAAVREFAKRCDVLTVEIEHVDVDTLEALEK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  92 -KYNVPQSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQLDE 170
Cdd:PLN02948 105 qGVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSRRLAYDGRGNAVAKTEEDLSS 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 171 ARELIANQE--CVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQENEHRNQVLFKTVVPA------RANHEQEARREVDKIT 242
Cdd:PLN02948 185 AVAALGGFErgLYAEKWAPFVKELAVMVARSRDGSTRCYPVVETIHKDNICHVVEAPAnvpwkvAKLATDVAEKAVGSLE 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 243 QAvhfvGTFTVEFFIDQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGHRLPEHIELLKPAIMMNLLGKD--- 319
Cdd:PLN02948 265 GA----GVFGVELFLLKDGQILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLGDTSMKVPAAIMYNILGEDege 340

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505960963 320 ------LDLLEKELfAHPDWHVHLYGKVSRKPERKMGHLTILTDDVSKTEQQL--IVKFEGRDEY 376
Cdd:PLN02948 341 agfrlaHQLMGRAL-NIPGASVHWYGKPEMRKQRKMGHITVVGPSAAEVEARLdqLLAEESADPD 404
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 116-282 2.08e-49

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 163.96  E-value: 2.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  116 AQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYDGKGQIRLTSEAQLDEARELIANQECVAEQFLDLAKEVSLT 195
Cdd:pfam02222   1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGYDGKGQYVVRSEADLPQAWEELGDGPVIVEEFVPFDRELSVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  196 VTIGNEGQMVYFPLQENEHRNQVLFKTVVPARANHEQEARRE--VDKITQAVHFVGTFTVEFFIDQQNELYVNEIAPRPH 273
Cdd:pfam02222  81 VVRSVDGETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQdiAKRLVDELGGVGVFGVELFVTEDGDLLINELAPRPH 160


                  ....*....
gi 505960963  274 NSGHYSIEA 282
Cdd:pfam02222 161 NSGHYTLDG 169
PurT COG0027
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ...
 16-350 3.95e-27

Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439798 [Multi-domain]  Cd Length: 393  Bit Score: 110.60  E-value: 3.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  16 GGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHefiHAAYDDM---PALERL--GERSDVITYEFENIAAEQLQTLV 90
Cdd:COG0027   19 GSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAH---RSYVIDMldgDALRALieREKPDFIVPEIEAIATDALVELE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  91 SK-YNVPQSYQAIQLLQDRltEK-QTLA--QAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGYdGKGQIRLTSEA 166
Cdd:COG0027   96 AEgFRVVPTARAVRLTMNR--EGiRRLAaeELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSS-GKGQSVVRSPA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 167 QLDEA-RELIAN-----QECVAEQFLDLAKEVSLtVTIGNEGQMVYF--PL---QENEH-----RNQVLFKTVVparanh 230
Cdd:COG0027  173 DIEAAwEYAQEGgrggaGRVIVEGFVDFDYEITL-LTVRAVDGPTHFcePIghrQEDGDyreswQPQPMSEAAL------ 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 231 eQEARREVDKITQAVHFVGTFTVEFFIdQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGhrLP-EHIELLKP 309
Cdd:COG0027  246 -AKAQEIAKKVTDALGGRGIFGVELFV-KGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILG--LPvPEIRLVGP 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 505960963 310 A----IMMNLLGKDL--DLLEKELfAHPDWHVHLYGKVSRKPERKMG 350
Cdd:COG0027  322 AasavILAEGESWAPafDGLAEAL-AVPGTDLRLFGKPEAYGRRRMG 367
purT PRK09288
formate-dependent phosphoribosylglycinamide formyltransferase;
16-350 2.53e-24

formate-dependent phosphoribosylglycinamide formyltransferase;


Pssm-ID: 236454 [Multi-domain]  Cd Length: 395  Bit Score: 102.91  E-value: 2.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  16 GGGQLGKMMAQSAQKMGFKVVVLDPDETCPCRYVAHEF--IhaaydDM---PALERL--GERSDVITYEFENIAAEQLQT 88
Cdd:PRK09288  19 GSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRShvI-----DMldgDALRAVieREKPDYIVPEIEAIATDALVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  89 LVSK-YNVPQSYQAIQLLQDRltEK-QTLA--QAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGyDGKGQIRLTS 164
Cdd:PRK09288  94 LEKEgFNVVPTARATRLTMNR--EGiRRLAaeELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS-SGKGQSVVRS 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 165 EAQLDEA-RELIANQ-----ECVAEQFLDLAKEVS-LTVTIGNEGqmVYF--PLqenEHRN---------QvlfktvvPA 226
Cdd:PRK09288 171 PEDIEKAwEYAQEGGrggagRVIVEEFIDFDYEITlLTVRAVDGG--THFcaPI---GHRQedgdyreswQ-------PQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 227 R--ANHEQEARREVDKITQAVHFVGTFTVEFFIdQQNELYVNEIAPRPHNSGHYSIEACDYSQFDTHILAVTGhrLP-EH 303
Cdd:PRK09288 239 PmsPAALEEAQEIAKKVTDALGGRGLFGVELFV-KGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILG--LPiPD 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505960963 304 IELLKPA----IMMNLLGKDL--DLLEKELfAHPDWHVHLYGKVSRKPERKMG 350
Cdd:PRK09288 316 IRLYSPAasavILAEGESANPsfDGLAEAL-AVPGTDVRLFGKPEIRGGRRMG 367
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 89-273 1.01e-21

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 93.40  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  89 LVSKYNVP-QSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRFGGyDGKGQIRLTSEAQ 167
Cdd:COG0439   35 LAEELGLPgPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGA-GSRGVRVVRDEEE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 168 LDEA-RELIA-------NQECVAEQFLDlAKEVSLTVtIGNEGQMVYFPLQEnEHRNQVLF---KTVVPARANHE--QEA 234
Cdd:COG0439  114 LEAAlAEARAeakagspNGEVLVEEFLE-GREYSVEG-LVRDGEVVVCSITR-KHQKPPYFvelGHEAPSPLPEElrAEI 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 505960963 235 RREVDKITQAVHFV-GTFTVEFFIDQQNELYVNEIAPRPH 273
Cdd:COG0439  191 GELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLG 230
PurK_C pfam17769
Phosphoribosylaminoimidazole carboxylase C-terminal domain; This entry represents the ...
 310-365 4.86e-18

Phosphoribosylaminoimidazole carboxylase C-terminal domain; This entry represents the C-terminal domain of the PurK enzyme.


Pssm-ID: 436029 [Multi-domain]  Cd Length: 56  Bit Score: 77.22  E-value: 4.86e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505960963  310 AIMMNLLGKDLDLLEKELFAHPDWHVHLYGKVSRKPERKMGHLTILTDDVSKTEQQ 365
Cdd:pfam17769   1 AVMVNLLGEELGEGLEELLAIPGAHLHLYGKEEARPGRKMGHVTVVGDDLEELLER 56
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 107-271 1.29e-10

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 60.40  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  107 DRLTEKQTLAQAGTKVVP--FVQVTSVADLDEAVQTLGFPFMLKTRFGGyDGKG--------QIRLTSEAQLDEARELIA 176
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPgtAGPVETEEEALAAAKEIGYPVIIKAAFGG-GGLGmgiarneeELAELFALALAEAPAAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  177 NQECVAEQFLDLAKEVSLTVTIGNEGQMVYFPLQEN--EHRNQvlfKTVVPARA-----NHEQEARREVDKITQAVHFVG 249
Cdd:pfam02786  80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECsdQRRTQ---KSIEVAPSqtltdEERQMLREAAVKIARHLGYVG 156

                         170       180
                  ....*....|....*....|...
gi 505960963  250 TFTVEFFIDQQN-ELYVNEIAPR 271
Cdd:pfam02786 157 AGTVEFALDPFSgEYYFIEMNTR 179
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 98-271 2.23e-09

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 58.50  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  98 SYQAIQLLQDRLTEKQTLAQAGTKVVPFVQvTSVADLDEAVQT---LGFPFMLKTRFGGyDGKGQIRLTSEAQLD----- 169
Cdd:PRK06111 106 SADIIAKMGSKIEARRAMQAAGVPVVPGIT-TNLEDAEEAIAIarqIGYPVMLKASAGG-GGIGMQLVETEQELTkafes 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 170 ---EARELIANQECVAEQFLDLAKEVSLTVTIGNEGQMVYfpLQENE----HRNQvlfKTVVPARANH-EQEARREVD-- 239
Cdd:PRK06111 184 nkkRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVY--LWEREcsvqRRHQ---KVIEEAPSPFlDEETRKAMGer 258

                        170       180       190
                 ....*....|....*....|....*....|....
gi 505960963 240 --KITQAVHFVGTFTVEFFIDQQNELYVNEIAPR 271
Cdd:PRK06111 259 avQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTR 292
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
98-271 2.37e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 55.49  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  98 SYQAIQLLQDRLTEKQTLAQAGTKVVPFVQvTSVADLDEAV---QTLGFPFMLKTRFGGyDGKGQIRLTSEAQL------ 168
Cdd:PRK07178 105 SAEVIRRMGDKTEARRAMIKAGVPVTPGSE-GNLADLDEALaeaERIGYPVMLKATSGG-GGRGIRRCNSREELeqnfpr 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 169 --DEARELIANQECVAEQFLDLAKEVSLTVTIGNEGQMVYfpLQEN----EHRNQVLFKTVVPARANHEQEAR--REVDK 240
Cdd:PRK07178 183 viSEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVH--LFERdcsiQRRNQKLIEIAPSPQLTPEQRAYigDLAVR 260

                        170       180       190
                 ....*....|....*....|....*....|.
gi 505960963 241 ITQAVHFVGTFTVEFFIDQQNELYVNEIAPR 271
Cdd:PRK07178 261 AAKAVGYENAGTVEFLLDADGEVYFMEMNTR 291
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 97-271 4.43e-08

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 54.98  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   97 QSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKtrfGGYDGKGQ--IRLTSEAQLDE--AR 172
Cdd:PRK12815  660 TSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIR---PSYVIGGQgmAVVYDEPALEAylAE 736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  173 ELIANQECVAEQFLDlAKEVSltVTIGNEGQMVYFPlQENEHrnqvLFKT---------VVPA---RANHEQEARREVDK 240
Cdd:PRK12815  737 NASQLYPILIDQFID-GKEYE--VDAISDGEDVTIP-GIIEH----IEQAgvhsgdsiaVLPPqslSEEQQEKIRDYAIK 808

                         170       180       190
                  ....*....|....*....|....*....|.
gi 505960963  241 ITQAVHFVGTFTVEFFIdQQNELYVNEIAPR 271
Cdd:PRK12815  809 IAKKLGFRGIMNIQFVL-ANDEIYVLEVNPR 838
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 98-264 7.97e-08

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 53.65  E-value: 7.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  98 SYQAIQLLQDRLTEKQTLAQAGTKVVPfvqvTS---VADLDEAVQ---TLGFPFMLKTRFGGyDGKGqIRL-TSEAQLDE 170
Cdd:PRK08591 106 SAETIRLMGDKVTAKATMKKAGVPVVP----GSdgpVDDEEEALAiakEIGYPVIIKATAGG-GGRG-MRVvRTEAELEK 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 171 ARElIANQECVA---------EQFLDLAKEVSLTVTIGNEGQMVYF-----PLQEnehRNQ-VLFKTVVPARAnheQEAR 235
Cdd:PRK08591 180 AFS-MARAEAKAafgnpgvymEKYLENPRHIEIQVLADGHGNAIHLgerdcSLQR---RHQkVLEEAPSPAIT---EELR 252

                        170       180       190
                 ....*....|....*....|....*....|...
gi 505960963 236 REVDKI----TQAVHFVGTFTVEFFIDQQNELY 264
Cdd:PRK08591 253 RKIGEAavkaAKAIGYRGAGTIEFLYEKNGEFY 285
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 95-271 6.46e-07

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 50.91  E-value: 6.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  95 VPQSYQAIQLLQDRLTEKQTLAQAGTKVVPFvQVTSVADLDEAVQ---TLGFPFMLKTRFGGyDGKGqIRLT-SEAQLde 170
Cdd:PRK12833 106 VGPDAQTIRTMGDKARARRTARRAGVPTVPG-SDGVVASLDAALEvaaRIGYPLMIKAAAGG-GGRG-IRVAhDAAQL-- 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 171 AREL-IANQECVA---------EQFLDLAKEVSLTVtIGNEGQMVYfpLQENE----HRNQVLFKTVVPARANHEQEAR- 235
Cdd:PRK12833 181 AAELpLAQREAQAafgdggvylERFIARARHIEVQI-LGDGERVVH--LFEREcslqRRRQKILEEAPSPSLTPAQRDAl 257

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505960963 236 -REVDKITQAVHFVGTFTVEF-FIDQQNELYVNEIAPR 271
Cdd:PRK12833 258 cASAVRLARQVGYRGAGTLEYlFDDARGEFYFIEMNTR 295
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 9-75 7.15e-07

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 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. 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. 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 hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. 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, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 50.32  E-value: 7.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDpdetcpcRYVAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd05198  140 GKTVGIVGLGRIGQRVAKRLQAFGMKVLYYD-------RTRKPEPEEDLGFRVVSLDELLAQSDVVV 199
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
 9-75 1.47e-06

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 49.44  E-value: 1.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcrYVAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd05299  142 GLTLGLVGFGRIGRAVAKRAKAFGFRVIAYDP-------YVPDGVAALGGVRVVSLDELLARSDVVS 201
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
99-271 1.50e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 49.71  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  99 YQAIQLLQDRLTEKQTLAQAGTKVVPFVQ--VTSVADLDEAVQTLGFPFMLKTRFGGyDGKGqIRLT-SEAQLDEARElI 175
Cdd:PRK05586 107 SETIELMGNKSNAREIMIKAGVPVVPGSEgeIENEEEALEIAKEIGYPVMVKASAGG-GGRG-IRIVrSEEELIKAFN-T 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 176 ANQECVA---------EQFLDLAKEVSLTVTIGNEGQMVYfpLQENE----HRNQVLFKTVVPARANheQEARREVDKIT 242
Cdd:PRK05586 184 AKSEAKAafgddsmyiEKFIENPKHIEFQILGDNYGNVVH--LGERDcslqRRNQKVLEEAPSPVMT--EELRKKMGEIA 259

                        170       180       190
                 ....*....|....*....|....*....|...
gi 505960963 243 ----QAVHFVGTFTVEFFIDQQNELYVNEIAPR 271
Cdd:PRK05586 260 vkaaKAVNYKNAGTIEFLLDKDGNFYFMEMNTR 292
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 9-75 2.87e-06

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 48.65  E-value: 2.87e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETcpcryvAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:COG0111  140 GKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK------PEEAADLGVGLVDSLDELLAEADVVS 200
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 9-75 3.58e-06

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: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 48.30  E-value: 3.58e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcrYVAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd12171  147 GKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDP-------YVDPEKIEADGVKKVSLEELLKRSDVVS 206
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 34-271 4.15e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 47.96  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  34 KVVVLDPDETCPCRYVAHEF--IHAAYDD--MPALERLGERSDV----ITYEFE---------NIAAEQLQTLVSkynvp 96
Cdd:PRK12767  27 RVIGADISELAPALYFADKFyvVPKVTDPnyIDRLLDICKKEKIdlliPLIDPElpllaqnrdRFEEIGVKVLVS----- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  97 qSYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQT--LGFPFMLKTRFGGyDGKGQIRLTSEAQLDEAREL 174
Cdd:PRK12767 102 -SKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKgeLQFPLFVKPRDGS-ASIGVFKVNDKEELEFLLEY 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 175 IAN---QECVAEQfldlakEVSLTVTIGNEGQMV-YFPLQenehRNQVLFKTVVPARANHEQEARREVDKITQAVHFVGT 250
Cdd:PRK12767 180 VPNliiQEFIEGQ------EYTVDVLCDLNGEVIsIVPRK----RIEVRAGETSKGVTVKDPELFKLAERLAEALGARGP 249

                        250       260
                 ....*....|....*....|.
gi 505960963 251 FTVEFFIDqQNELYVNEIAPR 271
Cdd:PRK12767 250 LNIQCFVT-DGEPYLFEINPR 269
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 114-271 7.89e-06

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 47.83  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  114 TLAQ-AGTKVVPFVQVTSVaDLDEAVQ---TLGFPFMLKTRFGGyDGKGQIRLTSEAQLDEA-----RELIA---NQECV 181
Cdd:PRK12999  125 NAAIkAGVPVIPGSEGPID-DIEEALEfaeEIGYPIMLKASAGG-GGRGMRIVRSEEELEEAferakREAKAafgNDEVY 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  182 AEQFLDLAK--EVSLtvtIG-NEGQMVYF-----PLQEnehRNQvlfKTVVPARANHEQEARRE------VdKITQAVHF 247
Cdd:PRK12999  203 LEKYVENPRhiEVQI---LGdKHGNVVHLyerdcSVQR---RHQ---KVVEIAPAPGLSEELREriceaaV-KLARAVGY 272

                         170       180
                  ....*....|....*....|....
gi 505960963  248 VGTFTVEFFIDQQNELYVNEIAPR 271
Cdd:PRK12999  273 VNAGTVEFLVDADGNFYFIEVNPR 296
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 98-271 8.97e-06

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 47.77  E-value: 8.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   98 SYQAIQLLQDRLTEKQTLAQAGTKVVPFVQ--VTSVADLDEAVQTLGFPFMLKTRFGGyDGKGQIRLTSEAQLDEA---- 171
Cdd:COG1038   109 SPEVLEMLGDKVAARAAAIEAGVPVIPGTEgpVDDLEEALAFAEEIGYPVMLKAAAGG-GGRGMRVVRSEEELEEAfesa 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  172 -RELIA---NQECVAEQFLDLAK--EVSLtvtIG-NEGQMVyfplqeneH----------RNQvlfKTVVPARANHEQEA 234
Cdd:COG1038   188 rREAKAafgDDEVFLEKYIERPKhiEVQI---LGdKHGNIV--------HlferdcsvqrRHQ---KVVEIAPAPNLDEE 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 505960963  235 RRE------VdKITQAVHFVGTFTVEFFIDQQNELYVNEIAPR 271
Cdd:COG1038   254 LREaiceaaV-KLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPR 295
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 9-75 5.31e-05

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: 43.25  E-value: 5.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963    9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcRYVAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDR------YPKPEEEEEELGARYVSLDELLAESDVVS 96
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 2-68 5.59e-05

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. 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 contains a host of activities, including the founding alcohol dehydrogenase (ADHs), 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: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 44.54  E-value: 5.59e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505960963   2 TFN-----KLQIGQTVGIIGGGQLGKMMAQSAQKMGFKVVVL--DPDETCPCRYV-AHEFIHAAYDDMP-ALERLG 68
Cdd:cd08296  152 TFNalrnsGAKPGDLVAVQGIGGLGHLAVQYAAKMGFRTVAIsrGSDKADLARKLgAHHYIDTSKEDVAeALQELG 227
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 9-75 6.92e-05

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 44.09  E-value: 6.92e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcrYV---AHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd12174  135 GKTLGVIGLGNIGRLVANAALALGMKVIGYDP-------YLsveAAWKLSVEVQRVTSLEELLATADYIT 197
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 2-75 8.75e-05

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: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 43.85  E-value: 8.75e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   2 TFNKLQI-GQTVGIIGGGQLGKMMAQSAqKMGF--KVVVLDPdetcpcrYVAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd12177  139 NFVGHELsGKTVGIIGYGNIGSRVAEIL-KEGFnaKVLAYDP-------YVSEEVIKKKGAKPVSLEELLAESDIIS 207
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 9-75 9.09e-05

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which 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.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 44.06  E-value: 9.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcryvaheFIHAAYDDMPA--LERLGERSDVIT 75
Cdd:cd12158  115 GKTVGIVGVGNVGSRLARRLEALGMNVLLCDP------------PRAEAEGDPGFvsLEELLAEADIIT 171
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 115-272 1.31e-04

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 42.69  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  115 LAQAGTKVVPFVQVTSVAD-------LDEAVQTLGFPFMLKTRFGGyDGKGQIRLTSEAQLDEARELIA--NQECVAEQF 185
Cdd:pfam07478   2 LKAAGLPVVPFVTFTRADWklnpkewCAQVEEALGYPVFVKPARLG-SSVGVSKVESREELQAAIEEAFqyDEKVLVEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  186 LDlAKEVSLTVtIGNEgQMVYFPLqeNEHRNQVLF------------KTVVPARANHEQEAR-RE-VDKITQAVHFVGTF 251
Cdd:pfam07478  81 IE-GREIECAV-LGNE-DPEVSPV--GEIVPSGGFydyeakyiddsaQIVVPADLEEEQEEQiQElALKAYKALGCRGLA 155

                         170       180
                  ....*....|....*....|.
gi 505960963  252 TVEFFIDQQNELYVNEIAPRP 272
Cdd:pfam07478 156 RVDFFLTEDGEIVLNEVNTIP 176
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 98-271 1.50e-04

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 43.71  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  98 SYQAIQLLQDRLTEKQTLAQAGTKVVPFVQVTSVADLDEAVQTLGFPFMLKTRF--GGyDGKGQIRltSEAQLDE----A 171
Cdd:COG0458  105 SPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYvlGG-RGMGIVY--NEEELEEylerA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 172 RELIANQECVAEQFLDLAKEVSL---------TVTIGNegqMvyfplqenEHrnqvlFK----------TVVPAR---AN 229
Cdd:COG0458  182 LKVSPDHPVLIDESLLGAKEIEVdvvrdgednVIIVGI---M--------EH-----IEpagvhsgdsiCVAPPQtlsDK 245

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 505960963 230 HEQEARREVDKITQAVHFVGTFTVEFFIDqQNELYVNEIAPR 271
Cdd:COG0458  246 EYQRLRDATLKIARALGVVGLCNIQFAVD-DGRVYVIEVNPR 286
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 9-75 2.22e-04

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. 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.


Pssm-ID: 240628 [Multi-domain]  Cd Length: 301  Bit Score: 42.52  E-value: 2.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcrYVAHE---FIHAAYDDmpaLERLGERSDVIT 75
Cdd:cd05303  139 GKTLGIIGFGRIGREVAKIARALGMNVIAYDP-------YPKDEqavELGVKTVS---LEELLKNSDFIS 198
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-42 2.46e-04

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (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 contains a host of 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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 42.31  E-value: 2.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 505960963   1 MTFNKLQIGQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDE 42
Cdd:cd05188  127 RRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSD 168
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 9-75 3.00e-04

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase 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. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. 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: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 42.29  E-value: 3.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDP-----DETCPCRYVahefihaayddmpALERLGERSDVIT 75
Cdd:cd01619  143 DQTVGVVGTGKIGRAVAQRAKGFGMKVIAYDPfrnpeLEDKGVKYV-------------SLEELFKNSDIIS 201
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
98-271 3.21e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 42.42  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963  98 SYQAIQLLQDRLTEKQTLAQAGTKVVPFVQvTSVADLDEA---VQTLGFPFMLKTRFGGyDGKGQIRLTSEAQLDEAReL 174
Cdd:PRK08462 108 SVEVMALMSDKSKAKEVMKRAGVPVIPGSD-GALKSYEEAkkiAKEIGYPVILKAAAGG-GGRGMRVVEDESDLENLY-L 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960963 175 IANQECVA---------EQFLDLAKEVSLTVTIGNEGQMVYF-----PLQEnehRNQVLFKTvVPARANHEQEARREVD- 239
Cdd:PRK08462 185 AAESEALSafgdgtmymEKFINNPRHIEVQILGDKHGNVIHVgerdcSLQR---RHQKLIEE-SPAVVLDEKTRERLHEt 260

                        170       180       190
                 ....*....|....*....|....*....|....
gi 505960963 240 --KITQAVHFVGTFTVEFFIDQQNELYVNEIAPR 271
Cdd:PRK08462 261 aiKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTR 294
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 5-42 3.23e-04

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 42.41  E-value: 3.23e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 505960963   5 KLQIGQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDE 42
Cdd:COG1064  159 GVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSP 196
XdhC_C pfam13478
XdhC Rossmann domain; This entry is the rossmann domain found in the Xanthine dehydrogenase ...
 14-74 4.16e-04

XdhC Rossmann domain; This entry is the rossmann domain found in the Xanthine dehydrogenase accessory protein.


Pssm-ID: 463891  Cd Length: 143  Bit Score: 40.17  E-value: 4.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505960963   14 IIGGGQLGKMMAQSAQKMGFKVVVLDPDETC--PCRYV-AHEFIHAAYDDMPALERLGERSDVI 74
Cdd:pfam13478   3 IFGAGHVAQALARLAALLGFRVTVVDPRPEFanPERFPdADEVIVWDLEEALELLRIDARTAVV 66
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
 9-75 4.51e-04

Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric.


Pssm-ID: 240646 [Multi-domain]  Cd Length: 308  Bit Score: 41.73  E-value: 4.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETcpcryvAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd12169  142 GKTLGIVGLGRIGARVARIGQAFGMRVIAWSSNLT------AERAAAAGVEAAVSKEELFATSDVVS 202
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 9-75 9.91e-04

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 40.55  E-value: 9.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcrYVAHEFIHAAYDDMPALERLGERSDVIT 75
Cdd:cd12172  142 GKTLGIIGLGRIGKAVARRLSGFGMKVLAYDP-------YPDEEFAKEHGVEFVSLEELLKESDFIS 201
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 9-75 1.38e-03

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share 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: 240659  Cd Length: 328  Bit Score: 40.12  E-value: 1.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPC-----RYVahefihaayddmpALERLGERSDVIT 75
Cdd:cd12183  144 GKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELaklgvEYV-------------DLDELLAESDIIS 202
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 9-75 1.85e-03

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 39.69  E-value: 1.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDpdetcpcRYVAHEF--IHAAYDDmpaLERLGERSDVIT 75
Cdd:COG1052  143 GKTLGIIGLGRIGQAVARRAKGFGMKVLYYD-------RSPKPEVaeLGAEYVS---LDELLAESDIVS 201
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 14-74 2.91e-03

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: 39.28  E-value: 2.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505960963  14 IIGGGQLGKMMAQSAQKMGFKVVVLDPDETCpCRYVAHEFIHAAYDD---MPALERLG-ERSDVI 74
Cdd:COG0569  100 IIGAGRVGRSLARELEEEGHDVVVIDKDPER-VERLAEEDVLVIVGDatdEEVLEEAGiEDADAV 163
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 9-42 3.04e-03

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 39.15  E-value: 3.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDE 42
Cdd:cd08254  166 GETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKE 199
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 1-74 5.28e-03

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. 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 contains a host of 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: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 38.63  E-value: 5.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   1 MTFNKLQIGQTVGIIGGGQLGKMMAQSAQKMGFKVVVL---DPDETCPCRYVAHEFIhaAYDDMPALERLGERSDVI 74
Cdd:cd05283  162 LKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFsrsPSKKEDALKLGADEFI--ATKDPEAMKKAAGSLDLI 236
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 5-42 6.03e-03

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 38.28  E-value: 6.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 505960963   5 KLQIGQTVGIIGGGQLGKMMAQSAQKMGF-KVVVLDPDE 42
Cdd:cd08234  156 GIKPGDSVLVFGAGPIGLLLAQLLKLNGAsRVTVAEPNE 194
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 9-75 7.68e-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: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 37.93  E-value: 7.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPdetcpcrYVAHEFihAAYDDMPA--LERLGERSDVIT 75
Cdd:cd12167  150 GRTVGIVGFGRIGRAVVELLRPFGLRVLVYDP-------YLPAAE--AAALGVELvsLDELLARSDVVS 209
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 9-75 9.29e-03

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: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 37.55  E-value: 9.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505960963   9 GQTVGIIGGGQLGKMMAQSAQKMGFKVVVLDPDETCPcryVAHEFIHAAYDDmpaLERLGERSDVIT 75
Cdd:cd12175  142 GKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPE---AEEKDLGVRYVE---LDELLAESDVVS 202
 
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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