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Conserved domains on  [gi|347591827|gb|AEP04548|]
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SDR family oxidoreductase [Acinetobacter baumannii MDR-ZJ06]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 1-246 2.96e-115

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05261:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 248  Bit Score: 335.10  E-value: 2.96e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFIAKNFIQFLSEKPEVEILKAHRETTDQEFEQVVLAADWIVHLAGVNRPLNEEEFAEGNTTLTEKISQIL 80
Cdd:cd05261    1 MKILITGAKGFIGKNLIARLKEQKDDDIFFYDRESDESELDDFLQGADFIFHLAGVNRPKDEAEFESGNVGLTERLLDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  81 QQANKKTPVILSSSIQVERDNPYGKSKLGGEQALVTLHQAQGNPVYICRLANVFGKWSRPNYNSAVATFCHNVANDLPLQ 160
Cdd:cd05261   81 TRNGKKPPILLSSSIQAALDNPYGKSKLAAEELLQEYARETGAPVYIYRLPNVFGKWCRPNYNSAVATFCYNIARDLPIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 161 IHDENAVIRLVYVDDVVETFWNILNGQQVEQ--FFQVEPEYQITVGDLAKVLNGFKASRGTLITDRVGTGLTRALYSTYL 238
Cdd:cd05261  161 INDPAAELTLVYIDDVVDELIQLLEGAPTYSggFDQVLPVYKVTVGEIAELLYKFKESRDTLILPNVGTGFDRALYSTYL 240


                 ....*...
gi 347591827 239 SFLKPEQF 246
Cdd:cd05261  241 SYLPPESF 248
cupin_CapF-like_C cd07007
Staphylococcus aureus CapF and related proteins, C-terminal cupin domain; This family contains ...
 257-365 1.65e-73

Staphylococcus aureus CapF and related proteins, C-terminal cupin domain; This family contains cupin domains of proteins homologous to Staphylococcus aureus CapF (also known as WbjC in Pseudomonas aeruginosa and FnlB in Escherichia coli). CapF is a bifunctional metalloenzyme produced by certain pathogenic bacteria and is essential in the biosynthetic path of capsular polysaccharide (CP), a mucous layer on the surface of bacterium that facilitates immune evasion and infection. Thus, CapF is an antibacterial/therapeutic target. In S. aureus, enzymes CapE, CapF and CapG catalyze the sequential transformation of UDP-D-GlcNAc in the CP precursor UDP-L-FucNAc via the intermediate compound UDP-N-acetyl-L-talosamine (UDP-L-TalNAc). CapF consists of two domains; the C-terminal cupin domain catalyzes the epimerization of the compound produced by the upstream enzyme CapE, and the N-terminal short-chain dehydrogenase/reductase (SDR) domain catalyzes the reduction of the compound afforded by the cupin domain, requiring one equivalent of NADPH. The cupin domain is crucial for catalyzing the first chemical reaction, and also important for the stability of the enzyme. Similarly, in P. aeruginosa, WbjC, WbjB and WbjD enzymes synthesize UDP-N-acetyl-L-fucosamine, a precursor of the lipopolysacharide component L-fucosamine. The cupin domains contain a conserved "jelly roll-like" beta-barrel fold.


:

Pssm-ID: 380410 [Multi-domain]  Cd Length: 109  Bit Score: 223.57  E-value: 1.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 257 RGVFVEMLKTPDAGQFSYFTAHPGITRGGHYHHTKTEKFLVIKGKALFKFKHVVTGEFYELETHGDEPRIVETVPGWTHD 336
Cdd:cd07007    1 RGSFTEFLKTPDSGQFSVSTTKPGITRGNHYHHTKNEKFLVIKGKALIRFRHIGTDEIIEYYVSGDKPEVVDIPPGYTHN 80

                         90       100
                 ....*....|....*....|....*....
gi 347591827 337 ITNIGDEEMVVMLWANEIFDRNKPDTYAM 365
Cdd:cd07007   81 ITNVGDDDLVTLFWANEIFDPNNPDTYFE 109
 
Name Accession Description Interval E-value
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
 1-246 2.96e-115

capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 335.10  E-value: 2.96e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFIAKNFIQFLSEKPEVEILKAHRETTDQEFEQVVLAADWIVHLAGVNRPLNEEEFAEGNTTLTEKISQIL 80
Cdd:cd05261    1 MKILITGAKGFIGKNLIARLKEQKDDDIFFYDRESDESELDDFLQGADFIFHLAGVNRPKDEAEFESGNVGLTERLLDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  81 QQANKKTPVILSSSIQVERDNPYGKSKLGGEQALVTLHQAQGNPVYICRLANVFGKWSRPNYNSAVATFCHNVANDLPLQ 160
Cdd:cd05261   81 TRNGKKPPILLSSSIQAALDNPYGKSKLAAEELLQEYARETGAPVYIYRLPNVFGKWCRPNYNSAVATFCYNIARDLPIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 161 IHDENAVIRLVYVDDVVETFWNILNGQQVEQ--FFQVEPEYQITVGDLAKVLNGFKASRGTLITDRVGTGLTRALYSTYL 238
Cdd:cd05261  161 INDPAAELTLVYIDDVVDELIQLLEGAPTYSggFDQVLPVYKVTVGEIAELLYKFKESRDTLILPNVGTGFDRALYSTYL 240


                 ....*...
gi 347591827 239 SFLKPEQF 246
Cdd:cd05261  241 SYLPPESF 248
cupin_CapF-like_C cd07007
Staphylococcus aureus CapF and related proteins, C-terminal cupin domain; This family contains ...
 257-365 1.65e-73

Staphylococcus aureus CapF and related proteins, C-terminal cupin domain; This family contains cupin domains of proteins homologous to Staphylococcus aureus CapF (also known as WbjC in Pseudomonas aeruginosa and FnlB in Escherichia coli). CapF is a bifunctional metalloenzyme produced by certain pathogenic bacteria and is essential in the biosynthetic path of capsular polysaccharide (CP), a mucous layer on the surface of bacterium that facilitates immune evasion and infection. Thus, CapF is an antibacterial/therapeutic target. In S. aureus, enzymes CapE, CapF and CapG catalyze the sequential transformation of UDP-D-GlcNAc in the CP precursor UDP-L-FucNAc via the intermediate compound UDP-N-acetyl-L-talosamine (UDP-L-TalNAc). CapF consists of two domains; the C-terminal cupin domain catalyzes the epimerization of the compound produced by the upstream enzyme CapE, and the N-terminal short-chain dehydrogenase/reductase (SDR) domain catalyzes the reduction of the compound afforded by the cupin domain, requiring one equivalent of NADPH. The cupin domain is crucial for catalyzing the first chemical reaction, and also important for the stability of the enzyme. Similarly, in P. aeruginosa, WbjC, WbjB and WbjD enzymes synthesize UDP-N-acetyl-L-fucosamine, a precursor of the lipopolysacharide component L-fucosamine. The cupin domains contain a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380410 [Multi-domain]  Cd Length: 109  Bit Score: 223.57  E-value: 1.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 257 RGVFVEMLKTPDAGQFSYFTAHPGITRGGHYHHTKTEKFLVIKGKALFKFKHVVTGEFYELETHGDEPRIVETVPGWTHD 336
Cdd:cd07007    1 RGSFTEFLKTPDSGQFSVSTTKPGITRGNHYHHTKNEKFLVIKGKALIRFRHIGTDEIIEYYVSGDKPEVVDIPPGYTHN 80

                         90       100
                 ....*....|....*....|....*....
gi 347591827 337 ITNIGDEEMVVMLWANEIFDRNKPDTYAM 365
Cdd:cd07007   81 ITNVGDDDLVTLFWANEIFDPNNPDTYFE 109
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2-210 8.60e-23

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 96.97  E-value: 8.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSEK-----------PEVEILKAHRE--------TTDQEFEQVVLAADWIVHLAGVNRPL-- 60
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARghevvgldrspPGAANLAALPGvefvrgdlRDPEALAAALAGVDAVVHLAAPAGVGee 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  61 NEEEFAEGNTTLTEKISQILQQANKKtPVILSSSIQV---------ERD-----NPYGKSKLGGEQALVTLHQAQGNPVY 126
Cdd:COG0451   81 DPDETLEVNVEGTLNLLEAARAAGVK-RFVYASSSSVygdgegpidEDTplrpvSPYGASKLAAELLARAYARRYGLPVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 127 ICRLANVFGkwsrPNYNSAVATFCHNVANDLPLQIH-DENAVIRLVYVDDVVETFWNIL-NGQQVEQFFQVEPEYQITVG 204
Cdd:COG0451  160 ILRPGNVYG----PGDRGVLPRLIRRALAGEPVPVFgDGDQRRDFIHVDDVARAIVLALeAPAAPGGVYNVGGGEPVTLR 235


                 ....*.
gi 347591827 205 DLAKVL 210
Cdd:COG0451  236 ELAEAI 241
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 3-184 1.87e-11

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 63.47  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827    3 VLVTGSNGFIAKNFIQFLSEKPEVEILKAHRETTDQEFEQVVL--------------------AADWIVHLAGV------ 56
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLrfvegdltdrdaleklladvRPDAVIHLAAVggvgas 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   57 -NRPlneEEFAEGNTTLTEKISQILQQANKKTPVILSSS--------IQVERD---------NPYGKSKLGGEQALVTLH 118
Cdd:pfam01370  81 iEDP---EDFIEANVLGTLNLLEAARKAGVKRFLFASSSevygdgaeIPQEETtltgplapnSPYAAAKLAGEWLVLAYA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347591827  119 QAQGNPVYICRLANVFGKW-SRPNYNSAVATFCHNVANDLPLQI-HDENAVIRLVYVDDVVETFWNIL 184
Cdd:pfam01370 158 AAYGLRAVILRLFNVYGPGdNEGFVSRVIPALIRRILEGKPILLwGDGTQRRDFLYVDDVARAILLAL 225
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 278-365 2.59e-06

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 45.73  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 278 HPGITRGGHYHHTKTEKFLVIKGKALfkfkhvvtgefYELETHGDEPRIVE----TV----PGWTHDITNIGDEEMVVML 349
Cdd:COG2140   11 EPGGVREEHWHPNAAEWYYVLSGEAR-----------MTVQDPPGRARTVDvgpgDVvyvpPGYGHYIINTGDEPLVFLA 79

                         90
                 ....*....|....*.
gi 347591827 350 WaneiFDRNKPDTYAM 365
Cdd:COG2140   80 V----FDDDAGSDYGT 91
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
 101-208 9.39e-05

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 44.35  E-value: 9.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 101 NPYGKSKLGGEQALVTLHQAQGNPVYICRLANVFGkwsrPNY--NSAVATFCHNVANDLPLQIH-DENAVIRLVYVDDVV 177
Cdd:PLN02260 157 NPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYG----PNQfpEKLIPKFILLAMQGKPLPIHgDGSNVRSYLYCEDVA 232

                         90       100       110
                 ....*....|....*....|....*....|.
gi 347591827 178 ETFWNILNGQQVEQFFQVEPEYQITVGDLAK 208
Cdd:PLN02260 233 EAFEVVLHKGEVGHVYNIGTKKERRVIDVAK 263
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 274-348 4.02e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 35.70  E-value: 4.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347591827  274 YFTAHPGITRGGHYHHTKTEKFLVIKGKALFkfkhVVTGEFYELEThGDeprIVETVPGWTHDITNIGDEEMVVM 348
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGEL----TVDGEEVVLKA-GD---SVYFPAGVPHRFRNTGDEPARLL 68
 
Name Accession Description Interval E-value
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
 1-246 2.96e-115

capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 335.10  E-value: 2.96e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFIAKNFIQFLSEKPEVEILKAHRETTDQEFEQVVLAADWIVHLAGVNRPLNEEEFAEGNTTLTEKISQIL 80
Cdd:cd05261    1 MKILITGAKGFIGKNLIARLKEQKDDDIFFYDRESDESELDDFLQGADFIFHLAGVNRPKDEAEFESGNVGLTERLLDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  81 QQANKKTPVILSSSIQVERDNPYGKSKLGGEQALVTLHQAQGNPVYICRLANVFGKWSRPNYNSAVATFCHNVANDLPLQ 160
Cdd:cd05261   81 TRNGKKPPILLSSSIQAALDNPYGKSKLAAEELLQEYARETGAPVYIYRLPNVFGKWCRPNYNSAVATFCYNIARDLPIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 161 IHDENAVIRLVYVDDVVETFWNILNGQQVEQ--FFQVEPEYQITVGDLAKVLNGFKASRGTLITDRVGTGLTRALYSTYL 238
Cdd:cd05261  161 INDPAAELTLVYIDDVVDELIQLLEGAPTYSggFDQVLPVYKVTVGEIAELLYKFKESRDTLILPNVGTGFDRALYSTYL 240


                 ....*...
gi 347591827 239 SFLKPEQF 246
Cdd:cd05261  241 SYLPPESF 248
cupin_CapF-like_C cd07007
Staphylococcus aureus CapF and related proteins, C-terminal cupin domain; This family contains ...
 257-365 1.65e-73

Staphylococcus aureus CapF and related proteins, C-terminal cupin domain; This family contains cupin domains of proteins homologous to Staphylococcus aureus CapF (also known as WbjC in Pseudomonas aeruginosa and FnlB in Escherichia coli). CapF is a bifunctional metalloenzyme produced by certain pathogenic bacteria and is essential in the biosynthetic path of capsular polysaccharide (CP), a mucous layer on the surface of bacterium that facilitates immune evasion and infection. Thus, CapF is an antibacterial/therapeutic target. In S. aureus, enzymes CapE, CapF and CapG catalyze the sequential transformation of UDP-D-GlcNAc in the CP precursor UDP-L-FucNAc via the intermediate compound UDP-N-acetyl-L-talosamine (UDP-L-TalNAc). CapF consists of two domains; the C-terminal cupin domain catalyzes the epimerization of the compound produced by the upstream enzyme CapE, and the N-terminal short-chain dehydrogenase/reductase (SDR) domain catalyzes the reduction of the compound afforded by the cupin domain, requiring one equivalent of NADPH. The cupin domain is crucial for catalyzing the first chemical reaction, and also important for the stability of the enzyme. Similarly, in P. aeruginosa, WbjC, WbjB and WbjD enzymes synthesize UDP-N-acetyl-L-fucosamine, a precursor of the lipopolysacharide component L-fucosamine. The cupin domains contain a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380410 [Multi-domain]  Cd Length: 109  Bit Score: 223.57  E-value: 1.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 257 RGVFVEMLKTPDAGQFSYFTAHPGITRGGHYHHTKTEKFLVIKGKALFKFKHVVTGEFYELETHGDEPRIVETVPGWTHD 336
Cdd:cd07007    1 RGSFTEFLKTPDSGQFSVSTTKPGITRGNHYHHTKNEKFLVIKGKALIRFRHIGTDEIIEYYVSGDKPEVVDIPPGYTHN 80

                         90       100
                 ....*....|....*....|....*....
gi 347591827 337 ITNIGDEEMVVMLWANEIFDRNKPDTYAM 365
Cdd:cd07007   81 ITNVGDDDLVTLFWANEIFDPNNPDTYFE 109
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 3-184 3.87e-28

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 108.93  E-value: 3.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   3 VLVTGSNGFIAKNFIQFLSEKPEVEIlkahrettdqefeqVVLAADWIVHLAGVNRP----LNEEEFAEGNTTLTEKISQ 78
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRLLERGHEVV--------------VIDRLDVVVHLAALVGVpaswDNPDEDFETNVVGTLNLLE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  79 ILQQANKKtPVILSSSIQV----------ERD-----NPYGKSKLGGEQALVTLHQAQGNPVYICRLANVFGKWSRPNYN 143
Cdd:cd08946   67 AARKAGVK-RFVYASSASVygspeglpeeEETpprplSPYGVSKLAAEHLLRSYGESYGLPVVILRLANVYGPGQRPRLD 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 347591827 144 SAVATFCHNVANDLPLQIHDENAVIR-LVYVDDVVETFWNIL 184
Cdd:cd08946  146 GVVNDFIRRALEGKPLTVFGGGNQTRdFIHVDDVVRAILHAL 187
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2-210 8.60e-23

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 96.97  E-value: 8.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSEK-----------PEVEILKAHRE--------TTDQEFEQVVLAADWIVHLAGVNRPL-- 60
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARghevvgldrspPGAANLAALPGvefvrgdlRDPEALAAALAGVDAVVHLAAPAGVGee 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  61 NEEEFAEGNTTLTEKISQILQQANKKtPVILSSSIQV---------ERD-----NPYGKSKLGGEQALVTLHQAQGNPVY 126
Cdd:COG0451   81 DPDETLEVNVEGTLNLLEAARAAGVK-RFVYASSSSVygdgegpidEDTplrpvSPYGASKLAAELLARAYARRYGLPVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 127 ICRLANVFGkwsrPNYNSAVATFCHNVANDLPLQIH-DENAVIRLVYVDDVVETFWNIL-NGQQVEQFFQVEPEYQITVG 204
Cdd:COG0451  160 ILRPGNVYG----PGDRGVLPRLIRRALAGEPVPVFgDGDQRRDFIHVDDVARAIVLALeAPAAPGGVYNVGGGEPVTLR 235


                 ....*.
gi 347591827 205 DLAKVL 210
Cdd:COG0451  236 ELAEAI 241
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 2-185 3.85e-15

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 75.08  E-value: 3.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSEKPEVEIL---KAHRETTDQEFEQV---------VLAADWIVHLAG---VNR---PLNEE 63
Cdd:cd05232    1 KVLVTGANGFIGRALVDKLLSRGEEVRIavrNAENAEPSVVLAELpdidsftdlFLGVDAVVHLAArvhVMNdqgADPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  64 EFAEGNTTLTEKISQILQQANKKTPVILSSsIQV-----------ERDNP-----YGKSKLGGEQALVTLHQAQGNPVYI 127
Cdd:cd05232   81 DYRKVNTELTRRLARAAARQGVKRFVFLSS-VKVngegtvgapfdETDPPapqdaYGRSKLEAERALLELGASDGMEVVI 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347591827 128 CRLANVFGKWSRPNYNS---AVATFchnvandLPLQIHDENAVIRLVYVDDVVETFWNILN 185
Cdd:cd05232  160 LRPPMVYGPGVRGNFARlmrLIDRG-------LPLPPGAVKNRRSLVSLDNLVDAIYLCIS 213
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 2-212 1.91e-13

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 69.94  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFI-QFLSEKPEVEIL----KAHRET---------------TDQEFEQVVLA-ADWIVHLA---GVN 57
Cdd:cd05256    1 RVLVTGGAGFIGSHLVeRLLERGHEVIVLdnlsTGKKENlpevkpnvkfiegdiRDDELVEFAFEgVDYVFHQAaqaSVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  58 RPLNEEEF-AEGNTTLTEKISQILQQANKKTPVILSSSI---------QVERD-----NPYGKSKLGGEQALVTLHQAQG 122
Cdd:cd05256   81 RSIEDPIKdHEVNVLGTLNLLEAARKAGVKRFVYASSSSvygdppylpKDEDHppnplSPYAVSKYAGELYCQVFARLYG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 123 NPVYICRLANVFGKWSRPN--YNSAVATFCHNVANDLPLQIH-DENAVIRLVYVDDVVETFWNILNGQQVEQFFQVEPEY 199
Cdd:cd05256  161 LPTVSLRYFNVYGPRQDPNggYAAVIPIFIERALKGEPPTIYgDGEQTRDFTYVEDVVEANLLAATAGAGGEVYNIGTGK 240

                        250
                 ....*....|...
gi 347591827 200 QITVGDLAKVLNG 212
Cdd:cd05256  241 RTSVNELAELIRE 253
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 3-184 1.87e-11

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 63.47  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827    3 VLVTGSNGFIAKNFIQFLSEKPEVEILKAHRETTDQEFEQVVL--------------------AADWIVHLAGV------ 56
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLrfvegdltdrdaleklladvRPDAVIHLAAVggvgas 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   57 -NRPlneEEFAEGNTTLTEKISQILQQANKKTPVILSSS--------IQVERD---------NPYGKSKLGGEQALVTLH 118
Cdd:pfam01370  81 iEDP---EDFIEANVLGTLNLLEAARKAGVKRFLFASSSevygdgaeIPQEETtltgplapnSPYAAAKLAGEWLVLAYA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347591827  119 QAQGNPVYICRLANVFGKW-SRPNYNSAVATFCHNVANDLPLQI-HDENAVIRLVYVDDVVETFWNIL 184
Cdd:pfam01370 158 AAYGLRAVILRLFNVYGPGdNEGFVSRVIPALIRRILEGKPILLwGDGTQRRDFLYVDDVARAILLAL 225
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
 2-195 9.04e-11

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 61.95  E-value: 9.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSEK-PEVEILKAH--RETTDQ--------------EFEQVVLAADWIVHLAGVNRPLNEE- 63
Cdd:cd05264    1 RVLIVGGNGFIGSHLVDALLEEgPQVRVFDRSipPYELPLggvdyikgdyenraDLESALVGIDTVIHLASTTNPATSNk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  64 ----EFaEGNTTLTEKISQILQQANKKTPVILSSSIQV----------ERD-----NPYGKSKLGGEQALVTLHQAQGNP 124
Cdd:cd05264   81 npilDI-QTNVAPTVQLLEACAAAGIGKIIFASSGGTVygvpeqlpisESDptlpiSSYGISKLAIEKYLRLYQYLYGLD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347591827 125 VYICRLANVFGKWSRPN-YNSAVATFCHNVANDLPLQIHDENAVIR-LVYVDDVVETFWNILNGQQVEQFFQV 195
Cdd:cd05264  160 YTVLRISNPYGPGQRPDgKQGVIPIALNKILRGEPIEIWGDGESIRdYIYIDDLVEALMALLRSKGLEEVFNI 232
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
2-185 4.86e-09

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 56.68  E-value: 4.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSEKPeVEILKAHRETTD----QEFEQVV--LAADWIVHLAG---VNRPLNEEEFAEG-NTT 71
Cdd:COG1091    1 RILVTGANGQLGRALVRLLAERG-YEVVALDRSELDitdpEAVAALLeeVRPDVVINAAAytaVDKAESEPELAYAvNAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  72 LTEKISQILQQANkkTPVILSSSIQV----------ERD--NP---YGKSKLGGEQALvtlhQAQGNPVYICRLANVFGK 136
Cdd:COG1091   80 GPANLAEACAELG--ARLIHISTDYVfdgtkgtpytEDDppNPlnvYGRSKLAGEQAV----RAAGPRHLILRTSWVYGP 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347591827 137 WSrpnyNSAVATFchnvandlpLQIHDENAVIRLV--------YVDDVVETFWNILN 185
Cdd:COG1091  154 HG----KNFVKTM---------LRLLKEGEELRVVddqigsptYAADLARAILALLE 197
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
 1-226 4.68e-08

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 54.09  E-value: 4.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFIAKNFIQFLSEK-PEVEI--------------LKAHRETTDQEFEQVVLA-------------ADWIVH 52
Cdd:cd05246    1 MKILVTGGAGFIGSNFVRYLLNKyPDYKIinldkltyagnlenLEDVSSSPRYRFVKGDICdaelvdrlfeeekIDAVIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  53 LAG---VNRPLNE-EEFAEGNTTLTekisQILQQANKKTPVIlsSSIQVERD---------------------NPYGKSK 107
Cdd:cd05246   81 FAAeshVDRSISDpEPFIRTNVLGT----YTLLEAARKYGVK--RFVHISTDevygdllddgeftetsplaptSPYSASK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 108 LGGEQALVTLHQAQGNPVYICRLANVFGKWSRPnyNSAVATFCHNVANDLPLQIHDENAVIR-LVYVDDVVETFWNILNG 186
Cdd:cd05246  155 AAADLLVRAYHRTYGLPVVITRCSNNYGPYQFP--EKLIPLFILNALDGKPLPIYGDGLNVRdWLYVEDHARAIELVLEK 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 347591827 187 QQVEQFFQVEPEYQITVGDLAKVL---NGFKASRGTLITDRVG 226
Cdd:cd05246  233 GRVGEIYNIGGGNELTNLELVKLIlelLGKDESLITYVKDRPG 275
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 2-184 6.56e-07

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 50.32  E-value: 6.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSEKPEVEILKAHRETTDQEFEQVVLAA----------DWIVHLAGVNRPLNEEEFAEG--- 68
Cdd:cd05254    1 KILITGATGMLGRALVRLLKERGYEVIGTGRSRASLFKLDLTDPDAveeairdykpDVIINCAAYTRVDKCESDPELayr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  69 -NTTLTEKISQILQQANkkTPVILSSSIQV---------ERD--NP---YGKSKLGGEQALvtlhQAQGNPVYICRLANV 133
Cdd:cd05254   81 vNVLAPENLARAAKEVG--ARLIHISTDYVfdgkkgpykEEDapNPlnvYGKSKLLGEVAV----LNANPRYLILRTSWL 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 347591827 134 FGKWSRPnyNSAVATFCHNVANDLPLQIhDENAVIRLVYVDDVVETFWNIL 184
Cdd:cd05254  155 YGELKNG--ENFVEWMLRLAAERKEVNV-VHDQIGSPTYAADLADAILELI 202
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 278-365 2.59e-06

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 45.73  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 278 HPGITRGGHYHHTKTEKFLVIKGKALfkfkhvvtgefYELETHGDEPRIVE----TV----PGWTHDITNIGDEEMVVML 349
Cdd:COG2140   11 EPGGVREEHWHPNAAEWYYVLSGEAR-----------MTVQDPPGRARTVDvgpgDVvyvpPGYGHYIINTGDEPLVFLA 79

                         90
                 ....*....|....*.
gi 347591827 350 WaneiFDRNKPDTYAM 365
Cdd:COG2140   80 V----FDDDAGSDYGT 91
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 272-348 6.27e-06

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 44.00  E-value: 6.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347591827 272 FSYFTAHPGITRGGHYHHTKTEKFLVIKGKALFkfkhVVTGEFYELEThGDeprIVETVPGWTHDITNIGDEEMVVM 348
Cdd:cd02221   21 FARVTLPPGSSIGYHQHEGEFEIYYILSGEGLY----TDNGKEYEVKA-GD---VTFTRDGESHGIENTGDEDLVFI 89
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 2-135 1.24e-05

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 46.37  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSE-KPEVEIL----KAHRET----------------TDQEFEQVVLAA---DWIVHLAG-- 55
Cdd:cd05247    1 KVLVTGGAGYIGSHTVVELLEaGYDVVVLdnlsNGHREAlpriekiriefyegdiRDRAALDKVFAEhkiDAVIHFAAlk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  56 -----VNRPLneeEFAEGNTTLTEKISQILQQANKKTpVILSSSIQV----------ERD-----NPYGKSKLGGEQALV 115
Cdd:cd05247   81 avgesVQKPL---KYYDNNVVGTLNLLEAMRAHGVKN-FVFSSSAAVygepetvpitEEAplnptNPYGRTKLMVEQILR 156

                        170       180
                 ....*....|....*....|
gi 347591827 116 TLHQAQGNPVYICRLANVFG 135
Cdd:cd05247  157 DLAKAPGLNYVILRYFNPAG 176
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 272-347 2.12e-05

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 42.08  E-value: 2.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347591827 272 FSYFTAHPGITRGGHYHHTKTEKFLVIKGKALFkfkHVVTGEFYELEThGDeprIVETVPGWTHDITNIGDEEMVV 347
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGEL---TLDDGETVELKA-GD---IVLIPPGVPHSFVNTSDEPAVF 69
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 1-212 5.18e-05

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: 44.20  E-value: 5.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFIAKNFIQFLSEK-----------------PEVEILKAHRETTDQEFEqvvLAA----DWIV-----HLA 54
Cdd:cd05265    1 MKILIIGGTRFIGKALVEELLAAghdvtvfnrgrtkpdlpEGVEHIVGDRNDRDALEE---LLGgedfDVVVdtiayTPR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  55 GVNRPLneeEFAEGNT---TLTEKIS---QILQQANKKTPVILSSSIQVERDNPYGKSKLGGEQALVTLHqaqGNPVYIC 128
Cdd:cd05265   78 QVERAL---DAFKGRVkqyIFISSASvylKPGRVITESTPLREPDAVGLSDPWDYGRGKRAAEDVLIEAA---AFPYTIV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 129 RLANVFGkwsrP-NYNSAVATFCHNVANDLPLQIHDENAVI-RLVYVDDVVETFWNIL-NGQQVEQFFQV-EPEYqITVG 204
Cdd:cd05265  152 RPPYIYG----PgDYTGRLAYFFDRLARGRPILVPGDGHSLvQFIHVKDLARALLGAAgNPKAIGGIFNItGDEA-VTWD 226

                        250
                 ....*....|..
gi 347591827 205 DL----AKVLNG 212
Cdd:cd05265  227 ELleacAKALGK 238
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
 101-208 9.39e-05

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 44.35  E-value: 9.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 101 NPYGKSKLGGEQALVTLHQAQGNPVYICRLANVFGkwsrPNY--NSAVATFCHNVANDLPLQIH-DENAVIRLVYVDDVV 177
Cdd:PLN02260 157 NPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYG----PNQfpEKLIPKFILLAMQGKPLPIHgDGSNVRSYLYCEDVA 232

                         90       100       110
                 ....*....|....*....|....*....|.
gi 347591827 178 ETFWNILNGQQVEQFFQVEPEYQITVGDLAK 208
Cdd:PLN02260 233 EAFEVVLHKGEVGHVYNIGTKKERRVIDVAK 263
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
 1-178 2.94e-04

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 42.32  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFIAKNFIQFLSEKPEVEI------------LKAHRETT---------------DQEFEQVVLAA---DWI 50
Cdd:cd05253    1 MKILVTGAAGFIGFHVAKRLLERGDEVVgidnlndyydvrLKEARLELlgksggfkfvkgdleDREALRRLFKDhefDAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  51 VHL---AGVNRPL-NEEEFAEGNTTLTEKISQILQQANKKTpVILSSSIQV----------ERDN------PYGKSKLGG 110
Cdd:cd05253   81 IHLaaqAGVRYSLeNPHAYVDSNIVGFLNLLELCRHFGVKH-LVYASSSSVyglntkmpfsEDDRvdhpisLYAATKKAN 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 347591827 111 EQALVTLHQAQGNPVYICRLANVFGKWSRPNYnsAVATFCHNVANDLPLQIHDENAVIR-LVYVDDVVE 178
Cdd:cd05253  160 ELMAHTYSHLYGIPTTGLRFFTVYGPWGRPDM--ALFLFTKAILEGKPIDVFNDGNMSRdFTYIDDIVE 226
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
 3-180 3.03e-04

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 42.42  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   3 VLVTGSNGFIAKNFIQFLSE----------------------KPEVEILKAhrETTDQEF-EQVVLAADWIVHLAGVNRP 59
Cdd:cd05241    2 VLVTGGSGFFGERLVKQLLErggtyvrsfdiappgealsawqHPNIEFLKG--DITDRNDvEQALSGADCVFHTAAIVPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  60 LNEEE-FAEGNTTLTEKISQILQQANKKTpVILSSSIQV-----------------ERDN-PYGKSKLGGEQALVTLHQA 120
Cdd:cd05241   80 AGPRDlYWEVNVGGTQNVLDACQRCGVQK-FVYTSSSSVifggqnihngdetlpypPLDSdMYAETKAIAEIIVLEANGR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347591827 121 QGNPVYICRLANVFGKWSR---PNYNSAVATfchnvANDLPlQIHDENAVIRLVYVDDVVETF 180
Cdd:cd05241  159 DDLLTCALRPAGIFGPGDQglvPILFEWAEK-----GLVKF-VFGRGNNLVDFTYVHNLAHAH 215
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
258-348 3.64e-04

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 39.74  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 258 GVFVEMLKTPDAGQFSYFTAHPGITRGGHYHHTKTEKFLVIKGKALFkfkhVVTGEFYELEThGDeprIVETVPGWTHDI 337
Cdd:COG0662   15 GSYEVLGEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEV----TIGDEEVELKA-GD---SVYIPAGVPHRL 86

                         90
                 ....*....|.
gi 347591827 338 TNIGDEEMVVM 348
Cdd:COG0662   87 RNPGDEPLELL 97
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 272-350 4.42e-04

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 38.37  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827 272 FSYFTAHPGITRGGHYHHTKtEKFLVIKGKALFkfkhVVTGEFYELEThGDeprIVETVPGWTHDITNIGDE--EMVVML 349
Cdd:cd06988    4 GAWCVVRPGTTSTPHSHHEY-EIFIVISGKGIV----VVDGEREPVKA-GD---VVYIPPGTEHYVKNDGDEdfEFYSIW 74


                 .
gi 347591827 350 W 350
Cdd:cd06988   75 W 75
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
 1-114 4.56e-04

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 41.60  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFIAKNFIQFLSEKPEVEILKAH--------------RETTDQEFEQVVLAA------DWIVHLAGVNRPL 60
Cdd:cd05238    1 MKVLITGASGFVGQRLAERLLSDVPNERLILIdvvspkapsgaprvTQIAGDLAVPALIEAlangrpDVVFHLAAIVSGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347591827  61 NEEEFAEG---NTTLTEKISQILQQANKKTPVILSSSIQVE--------RDNP-------YGKSKLGGEQAL 114
Cdd:cd05238   81 AEADFDLGyrvNVDGTRNLLEALRKNGPKPRFVFTSSLAVYglplpnpvTDHTaldpassYGAQKAMCELLL 152
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
1-122 4.92e-04

UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 41.54  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   1 MKVLVTGSNGFI----AKnfiQFLSEKPEVEIL----KAHRETTDQ--EFEQV----------VLAA---DWIVHLAG-- 55
Cdd:COG1087    1 MKILVTGGAGYIgshtVV---ALLEAGHEVVVLdnlsNGHREAVPKgvPFVEGdlrdraaldrVFAEhdiDAVIHFAAlk 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  56 -----VNRPLneeEFAEGNTTLTEKISQILQQANKKTpVILSSSIQV----------ERD-----NPYGKSKLGGEQALV 115
Cdd:COG1087   78 avgesVEKPL---KYYRNNVVGTLNLLEAMREAGVKR-FVFSSSAAVygepesvpitEDAptnptNPYGRSKLMVEQILR 153


                 ....*..
gi 347591827 116 TLHQAQG 122
Cdd:COG1087  154 DLARAYG 160
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
 2-94 6.07e-04

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. 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: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 41.06  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   2 KVLVTGSNGFIAKNFIQFLSEKP-EVEILKAHRETTDQEFEQVVLA-----------ADWIVHLAGvnRPLNEEEFAEGN 69
Cdd:cd05242    1 KIVITGGTGFIGRALTRRLTAAGhEVVVLSRRPGKAEGLAEVITWDglslgpwelpgADAVINLAG--EPIACRRWTEAN 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 347591827  70 --------TTLTEKISQILQQANKKTPVILSSS 94
Cdd:cd05242   79 kkeilssrIESTRVLVEAIANAPAPPKVLISAS 111
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 3-139 1.17e-03

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 40.36  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   3 VLVTGSNGFIAKNFIQFLSEKP-EV-----------EILKAHRETTDQEF--EQVVLAADW--------IVHLAG---VN 57
Cdd:cd05234    2 ILVTGGAGFIGSHLVDRLLEEGnEVvvvdnlssgrrENIEPEFENKAFRFvkRDLLDTADKvakkdgdtVFHLAAnpdVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  58 R-PLNEEEFAEGNTTLTEKISQILQQANKKTPVILSSS--------IQVERDNP------YGKSKLGGEQALVTLHQAQG 122
Cdd:cd05234   82 LgATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSStvygeakvIPTPEDYPplpisvYGASKLAAEALISAYAHLFG 161

                        170
                 ....*....|....*..
gi 347591827 123 NPVYICRLANVFGKWSR 139
Cdd:cd05234  162 FQAWIFRFANIVGPRST 178
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 3-178 2.82e-03

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 39.19  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827   3 VLVTGSNGFIAKNFIQFLSEKPE-VEILKahRETTDQEF---------------EQVVLAA----DWIVHLAGVNRPLN- 61
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQGYrVRALV--RSGSDAVLldglpvevvegdltdAASLAAAmkgcDRVFHLAAFTSLWAk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347591827  62 -EEEFAEGNTTLTEkisQILQQANKK--TPVILSSSIQV------------------ERDNPYGKSKLGGEQAlVTLHQA 120
Cdd:cd05228   79 dRKELYRTNVEGTR---NVLDAALEAgvRRVVHTSSIAAlggppdgridettpwnerPFPNDYYRSKLLAELE-VLEAAA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347591827 121 QGNPVYICRLANVFGKWSRPnyNSAVATFCHNVAND-LPlqihdenAVIR----LVYVDDVVE 178
Cdd:cd05228  155 EGLDVVIVNPSAVFGPGDEG--PTSTGLDVLDYLNGkLP-------AYPPggtsFVDVRDVAE 208
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 274-348 4.02e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 35.70  E-value: 4.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347591827  274 YFTAHPGITRGGHYHHTKTEKFLVIKGKALFkfkhVVTGEFYELEThGDeprIVETVPGWTHDITNIGDEEMVVM 348
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGEL----TVDGEEVVLKA-GD---SVYFPAGVPHRFRNTGDEPARLL 68
cupin_PGI cd02218
cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called ...
 285-350 8.14e-03

cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called cupin-like glucose-6-phosphate isomerase or cPGI; EC 5.3.1.9) family is found in archaea and certain prokaryotes where they catalyze the reversible aldose-ketose isomerization of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) as part of a unique variation of the Embden-Meyerhof glycolytic pathway. Cupin-PGIs represent a separate lineage in the evolution of phosphoglucose isomerases. Pyrococcus furiosus phosphoglucose isomerase (PfPGI) has been shown to be a metal-containing enzyme which catalyzes the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). These domains have a cupin beta-barrel fold capable of homodimerization.


Pssm-ID: 380347  Cd Length: 168  Bit Score: 36.77  E-value: 8.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347591827 285 GHYHHTKT--EKFLVIKGKALFKFKHVVTGEFYELE-THGDE---PrivetvPGWTHDITNIGDEEMVVMLW 350
Cdd:cd02218   66 GHYHAKRDypEVYEVLSGEGLLLLQKEDVGEVILVEaKPGDKvyiP------PGYAHRTINTGDEPLVFANW 131
 
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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