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Conserved domains on  [gi|515741966|ref|WP_017174566|]
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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]; ...
 2-402 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: 636.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADCI 81
Cdd:COG0452    5 KRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWADLI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  82 VVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAKGR 161
Cdd:COG0452   85 VIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 162 MEEPLQIVKIINDYFKDKNELShisytsfeGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAGP 241
Cdd:COG0452  165 MAEPEEIVEAIEALLAPKKDLA--------GKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 242 TQLDNPENVEVIHVESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQDGNLSVTFKRTKDILKYLGEHKT- 320
Cdd:COG0452  237 VALPTPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKp 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 321 HQYLVGFAAETQNINAYAQDKLKRKNADVIISNNVGDQTIGFQSDDNELTMHFKDGQRINIKKGKKVQLAQQILDELETR 400
Cdd:COG0452  317 GQFLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAEL 396


                 ..
gi 515741966 401 WQ 402
Cdd:COG0452  397 LA 398
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 2-402 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: 636.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADCI 81
Cdd:COG0452    5 KRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWADLI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  82 VVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAKGR 161
Cdd:COG0452   85 VIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 162 MEEPLQIVKIINDYFKDKNELShisytsfeGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAGP 241
Cdd:COG0452  165 MAEPEEIVEAIEALLAPKKDLA--------GKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 242 TQLDNPENVEVIHVESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQDGNLSVTFKRTKDILKYLGEHKT- 320
Cdd:COG0452  237 VALPTPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKp 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 321 HQYLVGFAAETQNINAYAQDKLKRKNADVIISNNVGDQTIGFQSDDNELTMHFKDGQRINIKKGKKVQLAQQILDELETR 400
Cdd:COG0452  317 GQFLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAEL 396


                 ..
gi 515741966 401 WQ 402
Cdd:COG0452  397 LA 398
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-402 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 556.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   1 MKNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADC 80
Cdd:PRK05579   6 GKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAKWADL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  81 IVVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAKG 160
Cdd:PRK05579  86 VLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGDVGPG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 161 RMEEPLQIVKIINDYFKDKnelshisytSFEGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAG 240
Cdd:PRK05579 166 RMAEPEEIVAAAERALSPK---------DLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 241 PTQLDNPENVEVIHVESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQDGNLSVTFKRTKDILKYLGEHKT 320
Cdd:PRK05579 237 PVNLPTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 321 HQ-YLVGFAAETQNINAYAQDKLKRKNADVIISNNVgDQTIGFQSDDNELTMHFKDGQRINIKKGKKVQLAQQILDELET 399
Cdd:PRK05579 317 KRpFVVGFAAETGDVLEYARAKLKRKGLDLIVANDV-SAGGGFGSDDNEVTLIWSDGGEVKLPLMSKLELARRLLDEIAE 395


                 ...
gi 515741966 400 RWQ 402
Cdd:PRK05579 396 RLL 398
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 2-397 3.44e-165

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: 468.39  E-value: 3.44e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966    2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTF--IEENPediQHIALGDWAD 79
Cdd:TIGR00521   4 KKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWgpIEHNA---LHIDLAKWAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   80 CIVVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAK 159
Cdd:TIGR00521  81 LILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  160 GRMEEPLQIVKIINDYFKDKNELshisytsfEGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVA 239
Cdd:TIGR00521 161 GRLAEPETIVKAAEREFSPKEDL--------EGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLIT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  240 GPTQLDNPENVEVIHVESAEEMFNAV-TSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQDGNLSVTFKRTKDILKYLGEH 318
Cdd:TIGR00521 233 GPVSLLTPPGVKSIKVSTAEEMLEAAlNELAKDFDIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  319 KTHQYLVGFAAETQN-INAYAQDKLKRKNADVIISNNVgDQTIGFQSDDNELTMHFKDGQRiNIKKGKKVQLAQQILDEL 397
Cdd:TIGR00521 313 KKHQVIVGFKAETNDdLIKYAKEKLKKKNLDMIVANDV-SQGRGFGSDENEVYIFSKHGHK-ELPLMSKLEVAERILDEI 390
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 190-370 7.02e-104

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: 304.72  E-value: 7.02e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  190 FEGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAGPTQLDNPENVEVIHVESAEEMFNAVTSRY 269
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  270 EEQDIVVKAAAVSDYTPADVLNHKMKKQDGN--LSVTFKRTKDILKYLGEHKTHQYLVGFAAETQNINAYAQDKLKRKNA 347
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSGGeeLTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKNL 160

                         170       180
                  ....*....|....*....|...
gi 515741966  348 DVIISNNVGDQTIGFQSDDNELT 370
Cdd:pfam04127 161 DLIVANDVSRPGAGFGSDTNEVT 183
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 195-319 6.18e-05

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: 44.20  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 195 ALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVA-GPTQLDNPENVE------------VIHVESAEEM 261
Cdd:cd05233    1 ALVTGA---------------SSG-IGRAIARRLAREGAKVVLADrNEEALAELAAIEalggnavavqadVSDEEDVEAL 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 262 FNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQ--DGNLSVTFKRTKDILKYLGEHK 319
Cdd:cd05233   65 VEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRvlDVNLTGVFLLTRAALPHMKKQG 124
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 2-402 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: 636.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADCI 81
Cdd:COG0452    5 KRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWADLI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  82 VVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAKGR 161
Cdd:COG0452   85 VIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 162 MEEPLQIVKIINDYFKDKNELShisytsfeGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAGP 241
Cdd:COG0452  165 MAEPEEIVEAIEALLAPKKDLA--------GKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 242 TQLDNPENVEVIHVESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQDGNLSVTFKRTKDILKYLGEHKT- 320
Cdd:COG0452  237 VALPTPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKp 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 321 HQYLVGFAAETQNINAYAQDKLKRKNADVIISNNVGDQTIGFQSDDNELTMHFKDGQRINIKKGKKVQLAQQILDELETR 400
Cdd:COG0452  317 GQFLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAEL 396


                 ..
gi 515741966 401 WQ 402
Cdd:COG0452  397 LA 398
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-402 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 556.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   1 MKNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADC 80
Cdd:PRK05579   6 GKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAKWADL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  81 IVVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAKG 160
Cdd:PRK05579  86 VLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGDVGPG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 161 RMEEPLQIVKIINDYFKDKnelshisytSFEGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAG 240
Cdd:PRK05579 166 RMAEPEEIVAAAERALSPK---------DLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 241 PTQLDNPENVEVIHVESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQDGNLSVTFKRTKDILKYLGEHKT 320
Cdd:PRK05579 237 PVNLPTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 321 HQ-YLVGFAAETQNINAYAQDKLKRKNADVIISNNVgDQTIGFQSDDNELTMHFKDGQRINIKKGKKVQLAQQILDELET 399
Cdd:PRK05579 317 KRpFVVGFAAETGDVLEYARAKLKRKGLDLIVANDV-SAGGGFGSDDNEVTLIWSDGGEVKLPLMSKLELARRLLDEIAE 395


                 ...
gi 515741966 400 RWQ 402
Cdd:PRK05579 396 RLL 398
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 2-397 3.44e-165

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: 468.39  E-value: 3.44e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966    2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTF--IEENPediQHIALGDWAD 79
Cdd:TIGR00521   4 KKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWgpIEHNA---LHIDLAKWAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   80 CIVVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAK 159
Cdd:TIGR00521  81 LILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  160 GRMEEPLQIVKIINDYFKDKNELshisytsfEGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVA 239
Cdd:TIGR00521 161 GRLAEPETIVKAAEREFSPKEDL--------EGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLIT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  240 GPTQLDNPENVEVIHVESAEEMFNAV-TSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQDGNLSVTFKRTKDILKYLGEH 318
Cdd:TIGR00521 233 GPVSLLTPPGVKSIKVSTAEEMLEAAlNELAKDFDIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  319 KTHQYLVGFAAETQN-INAYAQDKLKRKNADVIISNNVgDQTIGFQSDDNELTMHFKDGQRiNIKKGKKVQLAQQILDEL 397
Cdd:TIGR00521 313 KKHQVIVGFKAETNDdLIKYAKEKLKKKNLDMIVANDV-SQGRGFGSDENEVYIFSKHGHK-ELPLMSKLEVAERILDEI 390
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 2-381 1.22e-112

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 337.88  E-value: 1.22e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADCI 81
Cdd:PRK13982  71 KRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGHIRLARDCDLI 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  82 VVAPATANTIAKLSVGIADDIVTSTLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLA-CGYIAKG 160
Cdd:PRK13982 151 VVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIGPNAGEMAeRGEAGVG 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 161 RMEEPLQIVKIINDYFKDKNElshisyTSFEGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAG 240
Cdd:PRK13982 231 RMAEPLEIAAAAEALLRPPQP------KPLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAAAAGAEVTLISG 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 241 PTQLDNPENVEVIHVESAEEMFNAVTSRYeEQDIVVKAAAVSDYTPADVLNHKMKKQDGNL-SVTFKRTKDILKYLGEHK 319
Cdd:PRK13982 305 PVDLADPQGVKVIHVESARQMLAAVEAAL-PADIAIFAAAVADWRVATEGGQKLKKGAAGPpPLQLVENPDILATISKLA 383

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515741966 320 THQ--YLVGFAAETQNINAYAQDKLKRKNADVIISNNVGDQTIGFQSDDNELTMHFKDGQRINI 381
Cdd:PRK13982 384 ENRppLVIGFAAETEHLIDNARAKLARKGCDWIVANDVSPATGVMGGDRNTVHLLSRDGDAEKV 447
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 190-370 7.02e-104

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: 304.72  E-value: 7.02e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  190 FEGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAGPTQLDNPENVEVIHVESAEEMFNAVTSRY 269
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  270 EEQDIVVKAAAVSDYTPADVLNHKMKKQDGN--LSVTFKRTKDILKYLGEHKTHQYLVGFAAETQNINAYAQDKLKRKNA 347
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSGGeeLTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKNL 160

                         170       180
                  ....*....|....*....|...
gi 515741966  348 DVIISNNVGDQTIGFQSDDNELT 370
Cdd:pfam04127 161 DLIVANDVSRPGAGFGSDTNEVT 183
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 1-180 7.90e-81

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 246.01  E-value: 7.90e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   1 MKNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADC 80
Cdd:PRK07313   1 MKNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMNHIELAKRADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  81 IVVAPATANTIAKLSVGIADDIVTSTLLA--TETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIA 158
Cdd:PRK07313  81 FLVAPATANTIAKLAHGIADDLVTSVALAlpATTPKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEG 160

                        170       180
                 ....*....|....*....|..
gi 515741966 159 KGRMEEPLQIVKIINDYFKDKN 180
Cdd:PRK07313 161 YGALADIETILETIENTLKEKT 182
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 2-172 9.53e-61

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: 194.26  E-value: 9.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966    2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNPVYTNTFIEENPEDIQHIALGDWADCI 81
Cdd:TIGR02113   1 KKILLAVTGSIAAYKAADLTSQLTKLGYDVTVLMTQAATQFITPLTLQVLSKNPVHLDVMDEHDPKVINHIELAKKADLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   82 VVAPATANTIAKLSVGIADDIVTSTLLA--TETPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLACGYIAK 159
Cdd:TIGR02113  81 LVAPASANTIAHLAHGFADNIVTSVALAlpPETPKLIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGR 160

                         170
                  ....*....|...
gi 515741966  160 GRMEEPLQIVKII 172
Cdd:TIGR02113 161 GALADLDDILQTI 173
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 2-169 5.12e-44

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: 150.99  E-value: 5.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966    2 KNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQEFVTPLAFQAISRNpVYTNTFIEENPEDIQHIALG---DWA 78
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSEN-VDEDLTWRELDDDILHIELAsgaRWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   79 DCIVVAPATANTIAKLSVGIADDIVT----------------STLLATETPKFIAPAMNVHMYENKRTQHNISVLKDDEy 142
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLLTraadvalkerrphlenMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG- 158

                         170       180
                  ....*....|....*....|....*..
gi 515741966  143 hfiepgdgflacgyiAKGRMEEPLQIV 169
Cdd:pfam02441 159 ---------------GKGRMPEPEAIV 170
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
 196-371 1.07e-20

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 90.05  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 196 LVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAGPTQL--DNPENVEVIHVESAEEMFNAVTSRYEEQD 273
Cdd:PRK06732   4 LITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKTAVkpEPHPNLSIIEIENVDDLLETLEPLVKDHD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 274 IVVKAAAVSDYTP-----------ADVLNHKMKKQ--------DGNLSVTF-KRTKDILKYLGEHKTHQYLVGFA----A 329
Cdd:PRK06732  84 VLIHSMAVSDYTPvymtdleevsaSDNLNEFLTKQnteakissASDYQVLFlKKTPKVISYVKKWNPNITLVGFKllvnV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515741966 330 ETQNINAYAQDKLKRKNADVIISNNV----GDQTIGFQSDDNELTM 371
Cdd:PRK06732 164 SKEELIKVARASLIKNQADYILANDLtdisADQHKALLVSKNEVYT 209
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 4-168 7.04e-19

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 84.25  E-value: 7.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   4 ILLAVTGGIAAYKAIDLTSKLTQANyDVRVMLTDHAQEFVTPLAFqaisrnPVYTNTFIEENP--------EDIQHIALG 75
Cdd:PLN02496  22 ILLAASGSVAAIKFGNLCHCFSEWA-EVRAVVTKASLHFIDRASL------PKDVTLYTDEDEwsswnkigDSVLHIELR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  76 DWADCIVVAPATANTIAKLSVGIADDIVTSTLLATE--TPKFIAPAMNVHMYENKRTQHNISVLKDDEYHFIEPGDGFLA 153
Cdd:PLN02496  95 RWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAWDysKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLA 174

                        170
                 ....*....|....*
gi 515741966 154 CGYIAKGRMEEPLQI 168
Cdd:PLN02496 175 CGDYGNGAMAEPSLI 189
PRK09620 PRK09620
hypothetical protein; Provisional
 191-354 1.16e-10

hypothetical protein; Provisional


Pssm-ID: 181997  Cd Length: 229  Bit Score: 61.06  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 191 EGKHALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALAKRGAKVTLVAG-----PTQLDNpeNVEVIHVESAEEMFNAV 265
Cdd:PRK09620   2 KGKKVLITSGGCLEKWDQVRGHTNMAKGTIGRIIAEELISKGAHVIYLHGyfaekPNDINN--QLELHPFEGIIDLQDKM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 266 TS--RYEEQDIVVKAAAVSDYtpadvLNHKMKKQDGNLS-------------VTFKRTKDILKYLGEHKTHQYLVGFAAE 330
Cdd:PRK09620  80 KSiiTHEKVDAVIMAAAGSDW-----VVDKICDQEGNVLdmngkissdiapiIHFQKAPKVLKQIKQWDPETVLVGFKLE 154

                        170       180
                 ....*....|....*....|....*...
gi 515741966 331 TQN----INAYAQDKLKRKNADVIISNN 354
Cdd:PRK09620 155 SDVneeeLFERAKNRMEEAKASVMIANS 182
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 188-317 2.30e-07

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 51.35  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 188 TSFEGKHALVTAGptievidpvrfvsnrsSGKMGYAIAEALAKRGAKVtLVAGPTQLDNPENV---------EVIHV--- 255
Cdd:PRK05557   1 MSLEGKVALVTGA----------------SRGIGRAIAERLAAQGANV-VINYASSEAGAEALvaeigalggKALAVqgd 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515741966 256 ----ESAEEMFNAVTSRYEEQDIVVKAAAVSdytpADVLNHKMKKQD------GNLSVTFKRTKDILKYLGE 317
Cdd:PRK05557  64 vsdaESVERAVDEAKAEFGGVDILVNNAGIT----RDNLLMRMKEEDwdrvidTNLTGVFNLTKAVARPMMK 131
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
189-288 8.55e-07

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 49.87  E-value: 8.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 189 SFEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVA-GPTQLD--------NPENVEVIHV---- 255
Cdd:COG0300    2 SLTGKTVLITGA---------------SSG-IGRALARALAARGARVVLVArDAERLEalaaelraAGARVEVVALdvtd 65

                         90       100       110
                 ....*....|....*....|....*....|....
gi 515741966 256 -ESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPAD 288
Cdd:COG0300   66 pDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFE 99
AfpA COG1036
Archaeal flavoprotein [Energy production and conversion];
79-104 1.21e-06

Archaeal flavoprotein [Energy production and conversion];


Pssm-ID: 440659 [Multi-domain]  Cd Length: 174  Bit Score: 48.28  E-value: 1.21e-06
                         10        20
                 ....*....|....*....|....*.
gi 515741966  79 DCIVVAPATANTIAKLSVGIADDIVT 104
Cdd:COG1036   81 DTLVIAPATSNTVAKIVLGIADTLVT 106
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 188-288 1.41e-06

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: 49.01  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 188 TSFEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVA-GPTQLD------NPENVEVIHV----- 255
Cdd:COG1028    2 TRLKGKVALVTGG---------------SSG-IGRAIARALAAEGARVVITDrDAEALEaaaaelRAAGGRALAVaadvt 65

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515741966 256 --ESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPAD 288
Cdd:COG1028   66 deAAVEALVAAAVAAFGRLDILVNNAGITPPGPLE 100
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 212-291 4.64e-06

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: 47.43  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  212 VSNRSSgkMGYAIAEALAKRGAKVTLV-AGPTQLDNPE------NVEVIHV-----ESAEEMFNAVTSRYEEQDIVVKAA 279
Cdd:pfam13561   2 AANESG--IGWAIARALAEEGAEVVLTdLNEALAKRVEelaeelGAAVLPCdvtdeEQVEALVAAAVEKFGRLDILVNNA 79

                          90
                  ....*....|..
gi 515741966  280 AVSDYTPADVLN 291
Cdd:pfam13561  80 GFAPKLKGPFLD 91
PRK07326 PRK07326
SDR family oxidoreductase;
188-309 5.39e-06

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 47.31  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 188 TSFEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVAGPT--------QLDNPENV-----EVIH 254
Cdd:PRK07326   2 MSLKGKVALITGG---------------SKG-IGFAIAEALLAEGYKVAITARDQkeleeaaaELNNKGNVlglaaDVRD 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515741966 255 VESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQ--DGNLSVTFKRTK 309
Cdd:PRK07326  66 EADVQRAVDAIVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLviDTNLTGAFYTIK 122
PRK12826 PRK12826
SDR family oxidoreductase;
189-315 5.53e-05

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 44.14  E-value: 5.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 189 SFEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVAgpTQLDNPEN----------------VEV 252
Cdd:PRK12826   3 DLEGRVALVTGA---------------ARG-IGRAIAVRLAADGAEVIVVD--ICGDDAAAtaelveaaggkararqVDV 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515741966 253 IHVESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPA---------DVLnhkmkkqDGNLSVTFKRTKDILKYL 315
Cdd:PRK12826  65 RDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFaemddeqweRVI-------DVNLTGTFLLTQAALPAL 129
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 195-319 6.18e-05

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: 44.20  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 195 ALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVA-GPTQLDNPENVE------------VIHVESAEEM 261
Cdd:cd05233    1 ALVTGA---------------SSG-IGRAIARRLAREGAKVVLADrNEEALAELAAIEalggnavavqadVSDEEDVEAL 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 262 FNAVTSRYEEQDIVVKAAAVSDYTPADVLNHKMKKQ--DGNLSVTFKRTKDILKYLGEHK 319
Cdd:cd05233   65 VEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRvlDVNLTGVFLLTRAALPHMKKQG 124
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 192-332 1.00e-04

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical 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 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: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 43.40  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 192 GKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVA-------------GPTQLDNPENVEVIHV--- 255
Cdd:cd08939    1 GKHVLITGG---------------SSG-IGKALAKELVKEGANVIIVArseskleeaveeiEAEANASGQKVSYISAdls 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 256 --ESAEEMFNAVTSRYEEQDIVVKAAAVS------DYTPADVlnhkmKKQ-DGNLSVTFKRTKDILKYLGEHKTHQY--- 323
Cdd:cd08939   65 dyEEVEQAFAQAVEKGGPPDLVVNCAGISipglfeDLTAEEF-----ERGmDVNYFGSLNVAHAVLPLMKEQRPGHIvfv 139

                        170
                 ....*....|....
gi 515741966 324 -----LVGFAAETQ 332
Cdd:cd08939  140 ssqaaLVGIYGYSA 153
PRK09072 PRK09072
SDR family oxidoreductase;
217-284 1.06e-04

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 43.39  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 217 SGKMGYAIAEALAKRGAKVTLVA-GPTQLD-------NPENVEVIHV----ESAEEMFNAVTSRYEEQDIVVKAAAVSDY 284
Cdd:PRK09072  14 SGGIGQALAEALAAAGARLLLVGrNAEKLEalaarlpYPGRHRWVVAdltsEAGREAVLARAREMGGINVLINNAGVNHF 93
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
189-319 1.12e-04

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 43.22  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 189 SFEGKHALVTAGptievidpvrfvsnrsSGKMGYAIAEALAKRGAKVTLVA-GPTQLD--------NPENVEVIHV---- 255
Cdd:PRK05653   2 SLQGKTALVTGA----------------SRGIGRAIALRLAADGAKVVIYDsNEEAAEalaaelraAGGEARVLVFdvsd 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515741966 256 -ESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPAdvlnHKMKKQD------GNLSVTFKRTKDILKYLGEHK 319
Cdd:PRK05653  66 eAAVRALIEAAVEAFGALDILVNNAGITRDALL----PRMSEEDwdrvidVNLTGTFNVVRAALPPMIKAR 132
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 190-321 1.69e-04

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: 42.96  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 190 FEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLV---------------------AGPTQLD--N 246
Cdd:cd05369    1 LKGKVAFITGG---------------GTG-IGKAIAKAFAELGASVAIAgrkpevleaaaeeissatggrAHPIQCDvrD 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515741966 247 PENVEVIhVESAEEMFNAVtsryeeqDIVVKAAAVSDYTPADVLNHKMKKQ--DGNLSVTFKRTKDILKYLGEHKTH 321
Cdd:cd05369   65 PEAVEAA-VDETLKEFGKI-------DILINNAAGNFLAPAESLSPNGFKTviDIDLNGTFNTTKAVGKRLIEAKHG 133
PRK05920 PRK05920
aromatic acid decarboxylase; Validated
 1-104 1.80e-04

aromatic acid decarboxylase; Validated


Pssm-ID: 180312  Cd Length: 204  Bit Score: 42.14  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966   1 MKNILLAVTGGIAAYKAIDLTSKLTQANYDVRVMLTDHAQE-FVTPLAFQaISRNPVYTNTFIEE--NPEDIQHIALG-- 75
Cdd:PRK05920   3 MKRIVLAITGASGAIYGVRLLECLLAADYEVHLVISKAAQKvLATETGLK-LPAVPDLAEAFLREqlGAAAGQLRVHGkd 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 515741966  76 DWADCI----------VVAPATANTIAKLSVGIADDIVT 104
Cdd:PRK05920  82 DWGAPIasgsfrtdgmVIAPCSMGTLAAIAHGLSDNLIE 120
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 188-305 2.07e-04

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 42.55  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 188 TSFEGKHALVTAGptievidpvrfvsnrsSGKMGYAIAEALAKRGAKVTLVAGPTQLDNPENVEVIH------------- 254
Cdd:PRK12825   2 GSLMGRVALVTGA----------------ARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEalgrraqavqadv 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515741966 255 --VESAEEMFNAVTSRYEEQDIVVKAAAVS------DYTPAD---VLnhkmkkqDGNLSVTF 305
Cdd:PRK12825  66 tdKAALEAAVAAAVERFGRIDILVNNAGIFedkplaDMSDDEwdeVI-------DVNLSGVF 120
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 189-305 2.69e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 42.34  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 189 SFEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTL------VAGPTQLDNPEN-----VEVIHVES 257
Cdd:PRK06841  12 DLSGKVAVVTGG---------------ASG-IGHAIAELFAAKGARVALldrsedVAEVAAQLLGGNakglvCDVSDSQS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 515741966 258 AEEMFNAVTSRYEEQDIVVKAAAVSDYTPA-DV-LNHKMKKQDGNLSVTF 305
Cdd:PRK06841  76 VEAAVAAVISAFGRIDILVNSAGVALLAPAeDVsEEDWDKTIDINLKGSF 125
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 193-317 4.48e-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: 41.19  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 193 KHALVTAGptievidpvrfvsnrsSGKMGYAIAEALAKRGAKVTLVAGP------TQLDNPeNVEVIH-----VESAEEM 261
Cdd:cd08932    1 KVALVTGA----------------SRGIGIEIARALARDGYRVSLGLRNpedlaaLSASGG-DVEAVPydardPEDARAL 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515741966 262 FNAVTSRYEEQDIVVKAAAVSDYTP-ADVLNHKMKKQ-DGNLSVTFKRTKDILKYLGE 317
Cdd:cd08932   64 VDALRDRFGRIDVLVHNAGIGRPTTlREGSDAELEAHfSINVIAPAELTRALLPALRE 121
PRK07856 PRK07856
SDR family oxidoreductase;
189-288 7.47e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 40.69  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 189 SFEGKHALVTAGptievidpVRFVsnrssgkmGYAIAEALAKRGAKVtLVAGPTQLDNPENVEVIHV-------ESAEEM 261
Cdd:PRK07856   3 DLTGRVVLVTGG--------TRGI--------GAGIARAFLAAGATV-VVCGRRAPETVDGRPAEFHaadvrdpDQVAAL 65

                         90       100
                 ....*....|....*....|....*..
gi 515741966 262 FNAVTSRYEEQDIVVKAAAVSDYTPAD 288
Cdd:PRK07856  66 VDAIVERHGRLDVLVNNAGGSPYALAA 92
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 215-288 8.01e-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: 8.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 215 RSSGKMGYAIAEALAKRGAKVTLVAGptQLDNPENVEvihvesaeEMFNAVTSRYEEQDIVVKAAA------VSDYTPAD 288
Cdd:cd05359   30 RKSKDAAAEVAAEIEELGGKAVVVRA--DVSQPQDVE--------EMFAAVKERFGRLDVLVSNAAagafrpLSELTPAH 99
spoVFB PRK08305
dipicolinate synthase subunit B; Reviewed
 79-109 8.99e-04

dipicolinate synthase subunit B; Reviewed


Pssm-ID: 181370 [Multi-domain]  Cd Length: 196  Bit Score: 40.26  E-value: 8.99e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 515741966  79 DCIVVAPATANTIAKLSVGIADdivTSTLLA 109
Cdd:PRK08305  86 DCMVIAPCTGNTMAKLANAITD---SPVLMA 113
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 189-288 1.11e-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: 40.17  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 189 SFEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVA-GPTQLDN-----PENVEVIHV-----ES 257
Cdd:COG4221    2 SDKGKVALITGA---------------SSG-IGAATARALAAAGARVVLAArRAERLEAlaaelGGRALAVPLdvtdeAA 65

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515741966 258 AEEMFNAVTSRYEEQDIVVKAAAVSDYTPAD 288
Cdd:COG4221   66 VEAAVAAAVAEFGRLDVLVNNAGVALLGPLE 96
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 216-319 1.40e-03

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) 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: TGxxxGxG in classical SDRs. 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 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. 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-151 and Lys-155, and well as Asn-111 (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: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 39.84  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 216 SSGKMGYAIAEALAKRGAKVtlVAGPTQLDNPENVE----------------VIHVESAEEMFNAVTSRYEEQDIVVKAA 279
Cdd:cd05333    8 ASRGIGRAIALRLAAEGAKV--AVTDRSEEAAAETVeeikalggnaaaleadVSDREAVEALVEKVEAEFGPVDILVNNA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515741966 280 AVSdytpADVLNHKMKKQD------GNLSVTFKRTKDILKYLGEHK 319
Cdd:cd05333   86 GIT----RDNLLMRMSEEDwdavinVNLTGVFNVTQAVIRAMIKRR 127
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 217-291 2.62e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 39.20  E-value: 2.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515741966 217 SGKMGYAIAEALAKRGAKVTLVA-GPTQLDNPENVEVIHV--ESAEEMFNAVTSRyeEQDIVVKaaaVSDYTPADVLN 291
Cdd:cd05265    9 TRFIGKALVEELLAAGHDVTVFNrGRTKPDLPEGVEHIVGdrNDRDALEELLGGE--DFDVVVD---TIAYTPRQVER 81
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 190-287 2.88e-03

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 39.05  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 190 FEGKHALVTAGptievidpvrfvsnrsSGKMGYAIAEALAKRGAKVtLVAGPTQLD-----------NPENVEVIHV--- 255
Cdd:PRK05565   3 LMGKVAIVTGA----------------SGGIGRAIAELLAKEGAKV-VIAYDINEEaaqelleeikeEGGDAIAVKAdvs 65

                         90       100       110
                 ....*....|....*....|....*....|....
gi 515741966 256 --ESAEEMFNAVTSRYEEQDIVVKAAAVSDYTPA 287
Cdd:PRK05565  66 seEDVENLVEQIVEKFGKIDILVNNAGISNFGLV 99
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 192-239 4.83e-03

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. 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: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 38.41  E-value: 4.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515741966 192 GKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVA 239
Cdd:cd05344    1 GKVALVTAA---------------SSG-IGLAIARALAREGARVAICA 32
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 192-281 4.99e-03

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. 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: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 38.36  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 192 GKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLV-----------AGPTQLDNPENVEVIHV----- 255
Cdd:cd05327    1 GKVVVITGA---------------NSG-IGKETARELAKRGAHVIIAcrneekgeeaaAEIKKETGNAKVEVIQLdlssl 64

                         90       100
                 ....*....|....*....|....*.
gi 515741966 256 ESAEEMFNAVTSRYEEQDIVVKAAAV 281
Cdd:cd05327   65 ASVRQFAEEFLARFPRLDILINNAGI 90
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 188-276 6.91e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 37.96  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966 188 TSFEGKHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVAGPTQLDNPENVEVIH-----VESAEEMF 262
Cdd:PRK06523   5 LELAGKRALVTGG---------------TKG-IGAATVARLLEAGARVVTTARSRPDDLPEGVEFVAadlttAEGCAAVA 68

                         90
                 ....*....|....
gi 515741966 263 NAVTSRYEEQDIVV 276
Cdd:PRK06523  69 RAVLERLGGVDILV 82
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 193-290 9.85e-03

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 36.82  E-value: 9.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515741966  193 KHALVTAGptievidpvrfvsnrSSGkMGYAIAEALAKRGAKVTLVAGptqldNPENVEVIHVESAEEMFNA------VT 266
Cdd:pfam00106   1 KVALVTGA---------------SSG-IGRAIAKRLAKEGAKVVLVDR-----SEEKLEAVAKELGALGGKAlfiqgdVT 59

                          90       100
                  ....*....|....*....|....
gi 515741966  267 SRYEEQDIVvkAAAVSDYTPADVL 290
Cdd:pfam00106  60 DRAQVKALV--EQAVERLGRLDIL 81
 
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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