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Conserved domains on  [gi|739697947|ref|WP_037552330|]
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MULTISPECIES: bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC [Staphylococcus]

Protein Classification

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase( domain architecture ID 11418829)

bifunctional phosphopantothenoylcysteine decarboxylase (CoaC)/phosphopantothenate synthase (CoaB) catalyzes two steps in the biosynthesis of coenzyme A, the conjugation of cysteine to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, followed by its decarboxylation to form 4'-phosphopantotheine

EC:  4.1.1.36|6.3.2.5
Gene Ontology:  GO:0071513|GO:0010181|GO:0046872|GO:0004632|GO:0004633|GO:0015937|GO:0015941

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 2-399 0e+00

Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 631.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADAI 81
Cdd:COG0452    5 KRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWADLI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  82 VVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAKGR 161
Cdd:COG0452   85 VIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 162 MEEPSQIVKVLNDFFNSQKikeesSFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQL 241
Cdd:COG0452  165 MAEPEEIVEAIEALLAPKK-----DLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVAL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 242 TDPIDIDVVHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHKMKKQDGTLAVTFKRTKDILKYLGEHKGQ-QY 320
Cdd:COG0452  240 PTPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPgQF 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739697947 321 LVGFAAETQNIEAYAQDKLKRKNADVIISNNVGDKTIGFKSDDNELTMHFKSKEMINIKRGKKVQLAEQILDELETRWQ 399
Cdd:COG0452  320 LVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAELLA 398
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 2-399 0e+00

Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 631.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADAI 81
Cdd:COG0452    5 KRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWADLI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  82 VVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAKGR 161
Cdd:COG0452   85 VIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 162 MEEPSQIVKVLNDFFNSQKikeesSFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQL 241
Cdd:COG0452  165 MAEPEEIVEAIEALLAPKK-----DLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVAL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 242 TDPIDIDVVHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHKMKKQDGTLAVTFKRTKDILKYLGEHKGQ-QY 320
Cdd:COG0452  240 PTPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPgQF 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739697947 321 LVGFAAETQNIEAYAQDKLKRKNADVIISNNVGDKTIGFKSDDNELTMHFKSKEMINIKRGKKVQLAEQILDELETRWQ 399
Cdd:COG0452  320 LVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAELLA 398
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-399 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 554.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   1 MKHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADA 80
Cdd:PRK05579   6 GKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAKWADL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  81 IVVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAKG 160
Cdd:PRK05579  86 VLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGDVGPG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 161 RMEEPSQIVKVLNDFFNSQKikeessFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQ 240
Cdd:PRK05579 166 RMAEPEEIVAAAERALSPKD------LAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 241 LTDPIDIDVVHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHKMKKQDGTLAVTFKRTKDILKYLGEHKGQQ- 319
Cdd:PRK05579 240 LPTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKDKRp 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 320 YLVGFAAETQNIEAYAQDKLKRKNADVIISNNVgDKTIGFKSDDNELTMHFKSKEMINIKRGKKVQLAEQILDELETRWQ 399
Cdd:PRK05579 320 FVVGFAAETGDVLEYARAKLKRKGLDLIVANDV-SAGGGFGSDDNEVTLIWSDGGEVKLPLMSKLELARRLLDEIAERLL 398
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 2-394 9.20e-159

phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273116 [Multi-domain]  Cd Length: 391  Bit Score: 452.21  E-value: 9.20e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947    2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIqHIALGDWADAI 81
Cdd:TIGR00521   4 KKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWADLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   82 VVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAKGR 161
Cdd:TIGR00521  83 LIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEGKGR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  162 MEEPSQIVKVLNDFFNsqkikEESSFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQL 241
Cdd:TIGR00521 163 LAEPETIVKAAEREFS-----PKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  242 TDPIDIDVVHIESAEEMFEAVTTR-FDKQDIVIKAAAVSDYTPMEVLDHKMKKQDGTLAVTFKRTKDILKYLGEHKGQQY 320
Cdd:TIGR00521 238 LTPPGVKSIKVSTAEEMLEAALNElAKDFDIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKIKKHQV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739697947  321 LVGFAAETQN-IEAYAQDKLKRKNADVIISNNVgDKTIGFKSDDNELTMHFKSKEMiNIKRGKKVQLAEQILDEL 394
Cdd:TIGR00521 318 IVGFKAETNDdLIKYAKEKLKKKNLDMIVANDV-SQGRGFGSDENEVYIFSKHGHK-ELPLMSKLEVAERILDEI 390
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 187-367 2.07e-101

DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4.1.1.36) affects synthesis of DNA, and pantothenate metabolism.


Pssm-ID: 461186 [Multi-domain]  Cd Length: 183  Bit Score: 298.17  E-value: 2.07e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  187 FKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQLTDPIDIDVVHIESAEEMFEAVTTRF 266
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  267 DKQDIVIKAAAVSDYTPMEVLDHKMKKQDG--TLAVTFKRTKDILKYLGEHKGQQYLVGFAAETQNIEAYAQDKLKRKNA 344
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSGgeELTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKNL 160

                         170       180
                  ....*....|....*....|...
gi 739697947  345 DVIISNNVGDKTIGFKSDDNELT 367
Cdd:pfam04127 161 DLIVANDVSRPGAGFGSDTNEVT 183
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 192-290 3.22e-04

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 41.89  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 192 ALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV-------------TGPTQLTDPIDIDVVHIESAEEM 258
Cdd:cd05233    1 ALVTGA---------------SSG-IGRAIARRLAREGAKVVLAdrneealaelaaiEALGGNAVAVQADVSDEEDVEAL 64

                         90       100       110
                 ....*....|....*....|....*....|..
gi 739697947 259 FEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHK 290
Cdd:cd05233   65 VEEALEEFGRLDILVNNAGIARPGPLEELTDE 96
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 2-399 0e+00

Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 631.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADAI 81
Cdd:COG0452    5 KRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWADLI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  82 VVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAKGR 161
Cdd:COG0452   85 VIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 162 MEEPSQIVKVLNDFFNSQKikeesSFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQL 241
Cdd:COG0452  165 MAEPEEIVEAIEALLAPKK-----DLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVAL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 242 TDPIDIDVVHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHKMKKQDGTLAVTFKRTKDILKYLGEHKGQ-QY 320
Cdd:COG0452  240 PTPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPgQF 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739697947 321 LVGFAAETQNIEAYAQDKLKRKNADVIISNNVGDKTIGFKSDDNELTMHFKSKEMINIKRGKKVQLAEQILDELETRWQ 399
Cdd:COG0452  320 LVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAELLA 398
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-399 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 554.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   1 MKHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADA 80
Cdd:PRK05579   6 GKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAKWADL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  81 IVVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAKG 160
Cdd:PRK05579  86 VLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGDVGPG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 161 RMEEPSQIVKVLNDFFNSQKikeessFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQ 240
Cdd:PRK05579 166 RMAEPEEIVAAAERALSPKD------LAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 241 LTDPIDIDVVHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHKMKKQDGTLAVTFKRTKDILKYLGEHKGQQ- 319
Cdd:PRK05579 240 LPTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKDKRp 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 320 YLVGFAAETQNIEAYAQDKLKRKNADVIISNNVgDKTIGFKSDDNELTMHFKSKEMINIKRGKKVQLAEQILDELETRWQ 399
Cdd:PRK05579 320 FVVGFAAETGDVLEYARAKLKRKGLDLIVANDV-SAGGGFGSDDNEVTLIWSDGGEVKLPLMSKLELARRLLDEIAERLL 398
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 2-394 9.20e-159

phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273116 [Multi-domain]  Cd Length: 391  Bit Score: 452.21  E-value: 9.20e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947    2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIqHIALGDWADAI 81
Cdd:TIGR00521   4 KKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWADLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   82 VVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAKGR 161
Cdd:TIGR00521  83 LIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEGKGR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  162 MEEPSQIVKVLNDFFNsqkikEESSFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQL 241
Cdd:TIGR00521 163 LAEPETIVKAAEREFS-----PKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  242 TDPIDIDVVHIESAEEMFEAVTTR-FDKQDIVIKAAAVSDYTPMEVLDHKMKKQDGTLAVTFKRTKDILKYLGEHKGQQY 320
Cdd:TIGR00521 238 LTPPGVKSIKVSTAEEMLEAALNElAKDFDIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKIKKHQV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739697947  321 LVGFAAETQN-IEAYAQDKLKRKNADVIISNNVgDKTIGFKSDDNELTMHFKSKEMiNIKRGKKVQLAEQILDEL 394
Cdd:TIGR00521 318 IVGFKAETNDdLIKYAKEKLKKKNLDMIVANDV-SQGRGFGSDENEVYIFSKHGHK-ELPLMSKLEVAERILDEI 390
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 2-379 7.89e-110

bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Provisional


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 330.56  E-value: 7.89e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADAI 81
Cdd:PRK13982  71 KRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGHIRLARDCDLI 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  82 VVAPATANVIAKLSVGIADDILTSTLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLA-CGYVAKG 160
Cdd:PRK13982 151 VVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIGPNAGEMAeRGEAGVG 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 161 RMEEPSQIVKVLNDFFNSQkikEESSFKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQ 240
Cdd:PRK13982 231 RMAEPLEIAAAAEALLRPP---QPKPLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAAAAGAEVTLISGPVD 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 241 LTDPIDIDVVHIESAEEMFEAVTTRFdKQDIVIKAAAVSDYTPMEVLDHKMKKQD-GTLAVTFKRTKDILKYLGEHKGQQ 319
Cdd:PRK13982 308 LADPQGVKVIHVESARQMLAAVEAAL-PADIAIFAAAVADWRVATEGGQKLKKGAaGPPPLQLVENPDILATISKLAENR 386

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739697947 320 --YLVGFAAETQNIEAYAQDKLKRKNADVIISNNVGDKTIGFKSDDNelTMHFKSKEMINIK 379
Cdd:PRK13982 387 ppLVIGFAAETEHLIDNARAKLARKGCDWIVANDVSPATGVMGGDRN--TVHLLSRDGDAEK 446
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 187-367 2.07e-101

DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4.1.1.36) affects synthesis of DNA, and pantothenate metabolism.


Pssm-ID: 461186 [Multi-domain]  Cd Length: 183  Bit Score: 298.17  E-value: 2.07e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  187 FKGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQLTDPIDIDVVHIESAEEMFEAVTTRF 266
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  267 DKQDIVIKAAAVSDYTPMEVLDHKMKKQDG--TLAVTFKRTKDILKYLGEHKGQQYLVGFAAETQNIEAYAQDKLKRKNA 344
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSGgeELTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKNL 160

                         170       180
                  ....*....|....*....|...
gi 739697947  345 DVIISNNVGDKTIGFKSDDNELT 367
Cdd:pfam04127 161 DLIVANDVSRPGAGFGSDTNEVT 183
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 1-180 2.38e-81

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 247.17  E-value: 2.38e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   1 MKHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADA 80
Cdd:PRK07313   1 MKNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMNHIELAKRADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  81 IVVAPATANVIAKLSVGIADDILTSTLIA--TETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVA 158
Cdd:PRK07313  81 FLVAPATANTIAKLAHGIADDLVTSVALAlpATTPKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEG 160

                        170       180
                 ....*....|....*....|..
gi 739697947 159 KGRMEEPSQIVKVLNDFFNSQK 180
Cdd:PRK07313 161 YGALADIETILETIENTLKEKT 182
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 2-172 6.85e-62

phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single bifunctional protein catalyses phosphopantothenoylcysteine decarboxylase and phosphopantothenate--cysteine ligase activities, sequential steps in coenzyme A biosynthesis (see TIGR00521). These activities reside in separate proteins encoded by tandem genes in some bacterial lineages. This model describes proteins from the genera Streptococcus and Enterococcus homologous to the N-terminal region of TIGR00521, corresponding to phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 131168  Cd Length: 177  Bit Score: 197.34  E-value: 6.85e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947    2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQEIQHIALGDWADAI 81
Cdd:TIGR02113   1 KKILLAVTGSIAAYKAADLTSQLTKLGYDVTVLMTQAATQFITPLTLQVLSKNPVHLDVMDEHDPKVINHIELAKKADLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   82 VVAPATANVIAKLSVGIADDILTSTLIA--TETPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACGYVAK 159
Cdd:TIGR02113  81 LVAPASANTIAHLAHGFADNIVTSVALAlpPETPKLIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGR 160

                         170
                  ....*....|...
gi 739697947  160 GRMEEPSQIVKVL 172
Cdd:TIGR02113 161 GALADLDDILQTI 173
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 2-176 1.41e-42

Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyzes the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond. This family also includes the B chain of dipicolinate synthase a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance. dipicolinate synthase catalyzes the formation of dipicolinic acid from dihydroxydipicolinic acid. This family also includes phenyl-acrylic acid decarboxylase (EC:4.1.1.-).


Pssm-ID: 426775 [Multi-domain]  Cd Length: 177  Bit Score: 147.14  E-value: 1.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947    2 KHILLAVTGGIAAYKAIDLTSKLTQAGYDVRVMLSEHAQEFVTPLAFQAISRNPVYTNTFKEENPQeIQHIALG---DWA 78
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSENVDEDLTWRELDDD-ILHIELAsgaRWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   79 DAIVVAPATANVIAKLSVGIADDILT----------------STLIATETPKFIAPAMNVHMYENNRTQHNIKVLMQDGy 142
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLLTraadvalkerrphlenMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG- 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 739697947  143 hfiepgdgylacgyvAKGRMEEPSQIVKVLNDFF 176
Cdd:pfam02441 159 ---------------GKGRMPEPEAIVGKVLDAL 177
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 4-179 1.26e-21

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 91.96  E-value: 1.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947   4 ILLAVTGGIAAYKAIDLTSKLTQAGyDVRVMLSEHAQEFVTPLAFQaisrNPVYTNTFKEENPQ------EIQHIALGDW 77
Cdd:PLN02496  22 ILLAASGSVAAIKFGNLCHCFSEWA-EVRAVVTKASLHFIDRASLP----KDVTLYTDEDEWSSwnkigdSVLHIELRRW 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  78 ADAIVVAPATANVIAKLSVGIADDILTSTLIATE--TPKFIAPAMNVHMYENNRTQHNIKVLMQDGYHFIEPGDGYLACG 155
Cdd:PLN02496  97 ADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAWDysKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLACG 176

                        170       180
                 ....*....|....*....|....
gi 739697947 156 YVAKGRMEEPSQIVKVLNDFFNSQ 179
Cdd:PLN02496 177 DYGNGAMAEPSLIYSTVRLFLESR 200
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
 193-376 3.31e-21

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 91.20  E-value: 3.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 193 LVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTGPTQL--TDPIDIDVVHIESAEEMFEAVTTRFDKQD 270
Cdd:PRK06732   4 LITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKTAVkpEPHPNLSIIEIENVDDLLETLEPLVKDHD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 271 IVIKAAAVSDYTPM---------------EVLDH-----KMKKQDGTLAVTFKRTKDILKYLGEHKGQQYLVGFA----A 326
Cdd:PRK06732  84 VLIHSMAVSDYTPVymtdleevsasdnlnEFLTKqnteaKISSASDYQVLFLKKTPKVISYVKKWNPNITLVGFKllvnV 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739697947 327 ETQNIEAYAQDKLKRKNADVIISNNV----GDKTIGFKSDDNELTMhFKSKEMI 376
Cdd:PRK06732 164 SKEELIKVARASLIKNQADYILANDLtdisADQHKALLVSKNEVYT-AQTKEEI 216
PRK09620 PRK09620
hypothetical protein; Provisional
 188-351 2.66e-12

hypothetical protein; Provisional


Pssm-ID: 181997  Cd Length: 229  Bit Score: 66.07  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 188 KGKHALVTAGPTVEVIDPVRFVSNRSSGKMGYALAEALRNRGAHVTLVTG-----PTQLTDPIDIDVVH--IESAEEMFE 260
Cdd:PRK09620   2 KGKKVLITSGGCLEKWDQVRGHTNMAKGTIGRIIAEELISKGAHVIYLHGyfaekPNDINNQLELHPFEgiIDLQDKMKS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 261 AVTTrfDKQDIVIKAAAVSDYTPMEVLDhkmkkQDGTL-------------AVTFKRTKDILKYLGEHKGQQYLVGFAAE 327
Cdd:PRK09620  82 IITH--EKVDAVIMAAAGSDWVVDKICD-----QEGNVldmngkissdiapIIHFQKAPKVLKQIKQWDPETVLVGFKLE 154

                        170       180
                 ....*....|....*....|....*...
gi 739697947 328 TQNIEAY----AQDKLKRKNADVIISNN 351
Cdd:PRK09620 155 SDVNEEElferAKNRMEEAKASVMIANS 182
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
186-288 1.49e-05

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 46.02  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 186 SFKGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV----------------TGPTqlTDPIDIDV 249
Cdd:COG0300    2 SLTGKTVLITGA---------------SSG-IGRALARALAARGARVVLVardaerlealaaelraAGAR--VEVVALDV 63

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 739697947 250 VHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLD 288
Cdd:COG0300   64 TDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFEELD 102
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 185-285 5.50e-05

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 44.39  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 185 SSFKGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV----------------TGPTqlTDPIDID 248
Cdd:COG1028    2 TRLKGKVALVTGG---------------SSG-IGRAIARALAAEGARVVITdrdaealeaaaaelraAGGR--ALAVAAD 63

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 739697947 249 VVHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPME 285
Cdd:COG1028   64 VTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLE 100
AfpA COG1036
Archaeal flavoprotein [Energy production and conversion];
79-104 7.36e-05

Archaeal flavoprotein [Energy production and conversion];


Pssm-ID: 440659 [Multi-domain]  Cd Length: 174  Bit Score: 42.88  E-value: 7.36e-05
                         10        20
                 ....*....|....*....|....*.
gi 739697947  79 DAIVVAPATANVIAKLSVGIADDILT 104
Cdd:COG1036   81 DTLVIAPATSNTVAKIVLGIADTLVT 106
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 209-288 1.89e-04

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 42.42  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947  209 VSNRSSgkMGYALAEALRNRGAHVTLV-------TGPTQLTDPIDIDVVHI-----ESAEEMFEAVTTRFDKQDIVIKAA 276
Cdd:pfam13561   2 AANESG--IGWAIARALAEEGAEVVLTdlnealaKRVEELAEELGAAVLPCdvtdeEQVEALVAAAVEKFGRLDILVNNA 79

                          90
                  ....*....|..
gi 739697947  277 AVSDYTPMEVLD 288
Cdd:pfam13561  80 GFAPKLKGPFLD 91
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 192-290 3.22e-04

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 41.89  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 192 ALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV-------------TGPTQLTDPIDIDVVHIESAEEM 258
Cdd:cd05233    1 ALVTGA---------------SSG-IGRAIARRLAREGAKVVLAdrneealaelaaiEALGGNAVAVQADVSDEEDVEAL 64

                         90       100       110
                 ....*....|....*....|....*....|..
gi 739697947 259 FEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHK 290
Cdd:cd05233   65 VEEALEEFGRLDILVNNAGIARPGPLEELTDE 96
PRK07326 PRK07326
SDR family oxidoreductase;
185-287 3.35e-04

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 41.92  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 185 SSFKGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLVT-------------GPTQLTDPIDIDVVH 251
Cdd:PRK07326   2 MSLKGKVALITGG---------------SKG-IGFAIAEALLAEGYKVAITArdqkeleeaaaelNNKGNVLGLAADVRD 65

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 739697947 252 IESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVL 287
Cdd:PRK07326  66 EADVQRAVDAIVAAFGGLDVLIANAGVGHFAPVEEL 101
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 189-305 3.60e-04

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 41.98  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 189 GKHALVTAgptvevidpvrfVSNRssGKMGYALAEALRNRGAHV----------TLVTGPTQLTDPI------------- 245
Cdd:PRK12748   5 KKIALVTG------------ASRL--NGIGAAVCRRLAAKGIDIfftywspydkTMPWGMHDKEPVLlkeeiesygvrce 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739697947 246 --DIDVVHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLDHKMkkQDGTLAVTFKRT 305
Cdd:PRK12748  71 hmEIDLSQPYAPNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQ--LDKHYAVNVRAT 130
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 186-305 4.08e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 41.57  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 186 SFKGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV------------TGPTQLTdPIDIDVVHIE 253
Cdd:PRK06841  12 DLSGKVAVVTGG---------------ASG-IGHAIAELFAAKGARVALLdrsedvaevaaqLLGGNAK-GLVCDVSDSQ 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739697947 254 SAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEvlDHKMKKQDGTLAVTFKRT 305
Cdd:PRK06841  75 SVEAAVAAVISAFGRIDILVNSAGVALLAPAE--DVSEEDWDKTIDINLKGS 124
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 212-317 6.55e-04

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 40.80  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 212 RSSGKMGYALAEALRNRGAHVTLVTGptqltdpidiDVVHIESAEEMFEAVTTRFDKQDIVIKAAA------VSDYTPME 285
Cdd:cd05359   30 RKSKDAAAEVAAEIEELGGKAVVVRA----------DVSQPQDVEEMFAAVKERFGRLDVLVSNAAagafrpLSELTPAH 99

                         90       100       110
                 ....*....|....*....|....*....|..
gi 739697947 286 vLDHKMkkqDGTLAVTFKRTKDILKYLGEHKG 317
Cdd:cd05359  100 -WDAKM---NTNLKALVHCAQQAAKLMRERGG 127
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 190-314 6.75e-04

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 40.81  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 190 KHALVTAGptvevidpvrfvsnrsSGKMGYALAEALRNRGAHVTLVTGPTQLTD----------PIDIDVVHIESAEEMF 259
Cdd:cd08932    1 KVALVTGA----------------SRGIGIEIARALARDGYRVSLGLRNPEDLAalsasggdveAVPYDARDPEDARALV 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 739697947 260 EAVTTRFDKQDIVIKAAAVSDYTP-MEVLDHKMKKQ-DGTLAVTFKRTKDILKYLGE 314
Cdd:cd08932   65 DALRDRFGRIDVLVHNAGIGRPTTlREGSDAELEAHfSINVIAPAELTRALLPALRE 121
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 214-288 8.85e-04

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 40.26  E-value: 8.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739697947 214 SGKMGYALAEALRNRGAHVTLVtGPTQLTDPIDIDvvHIESAEEMFEAVttrfDKQDIVIKAAAVSDYTPMEVLD 288
Cdd:cd11731    7 TGTIGLAVAQLLSAHGHEVITA-GRSSGDYQVDIT--DEASIKALFEKV----GHFDAIVSTAGDAEFAPLAELT 74
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 187-277 1.09e-03

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 40.26  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 187 FKGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV----------------TGPTQLtDPIDIDVV 250
Cdd:cd05369    1 LKGKVAFITGG---------------GTG-IGKAIAKAFAELGASVAIAgrkpevleaaaeeissATGGRA-HPIQCDVR 63

                         90       100
                 ....*....|....*....|....*..
gi 739697947 251 HIESAEEMFEAVTTRFDKQDIVIKAAA 277
Cdd:cd05369   64 DPEAVEAAVDETLKEFGKIDILINNAA 90
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 208-287 1.19e-03

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 40.18  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 208 FVSNRSSGkMGYALAEALRNRGAHVTLVT----GPTQLTD-------PIDIDVVHIESAEEMFEAVTTRFDKQDIVIKAA 276
Cdd:cd08929    4 LVTGASRG-IGEATARLLHAEGYRVGICArdeaRLAAAAAqelegvlGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNA 82

                         90
                 ....*....|.
gi 739697947 277 AVSDYTPMEVL 287
Cdd:cd08929   83 GVGVMKPVEEL 93
PRK12826 PRK12826
SDR family oxidoreductase;
186-288 2.10e-03

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 39.51  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 186 SFKGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLVT----------------GPTQLTdpIDIDV 249
Cdd:PRK12826   3 DLEGRVALVTGA---------------ARG-IGRAIAVRLAADGAEVIVVDicgddaaataelveaaGGKARA--RQVDV 64

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 739697947 250 VHIESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLD 288
Cdd:PRK12826  65 RDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEMD 103
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
188-284 2.97e-03

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 39.24  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 188 KGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV--------TGPTQLTDP---IDIDVVHIESAE 256
Cdd:PRK07067   5 QGKVALLTGA---------------ASG-IGEAVAERYLAEGARVVIAdikpararLAALEIGPAaiaVSLDVTRQDSID 68

                         90       100
                 ....*....|....*....|....*...
gi 739697947 257 EMFEAVTTRFDKQDIVIKAAAVSDYTPM 284
Cdd:PRK07067  69 RIVAAAVERFGGIDILFNNAALFDMAPI 96
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 186-288 4.15e-03

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 38.62  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739697947 186 SFKGKHALVTAGptvevidpvrfvsnrSSGkMGYALAEALRNRGAHVTLV-------------TGPTQLtdPIDIDVVHI 252
Cdd:COG4221    2 SDKGKVALITGA---------------SSG-IGAATARALAAAGARVVLAarraerlealaaeLGGRAL--AVPLDVTDE 63

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 739697947 253 ESAEEMFEAVTTRFDKQDIVIKAAAVSDYTPMEVLD 288
Cdd:COG4221   64 AAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELD 99
 
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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