Domain of unknown function (DUF334); Staphylococcus aureus plasmid proteins with no characterized function.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2595077938  31 DTEELKDILGRDIYRVREENDRMLQEVRASHEHYKKRQKQLFTGIGAMLLVFMLFALIMTIGSDFMSFLHVDILQKAIAS 110
Cdd:pfam03904   1 EAPDVADTFKKDSYTVREETKKMLDEVNKSHEDYQKYKKIAVIGIGAMLLVFMLFALVMTIGNDFMEFLHVDHLQEAIAS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2595077938 111 KIRASEGFMTFVWYIAYGLPYILSIGLFIGLYEWIRAKFHD 151
Cdd:pfam03904  81 KMKASEGFITVLWYIAYGLPYILAIGIFIYLYEWIRRRFML 121

Domain of unknown function (DUF334); Staphylococcus aureus plasmid proteins with no characterized function.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2595077938  31 DTEELKDILGRDIYRVREENDRMLQEVRASHEHYKKRQKQLFTGIGAMLLVFMLFALIMTIGSDFMSFLHVDILQKAIAS 110
Cdd:pfam03904   1 EAPDVADTFKKDSYTVREETKKMLDEVNKSHEDYQKYKKIAVIGIGAMLLVFMLFALVMTIGNDFMEFLHVDHLQEAIAS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2595077938 111 KIRASEGFMTFVWYIAYGLPYILSIGLFIGLYEWIRAKFHD 151
Cdd:pfam03904  81 KMKASEGFITVLWYIAYGLPYILAIGIFIYLYEWIRRRFML 121

3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. 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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2595077938  96 MSFLHVDILqkaIASKIRASEGFMTFVWYIAYGLPYILSIGLFIGLYEWIR 146
Cdd:cd09812   209 VEFVHVDNL---VQAHILAAEALTTAKGYIASGQAYFISDGRPVNNFEFFR 256

Domain of unknown function (DUF334); Staphylococcus aureus plasmid proteins with no characterized function.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2595077938  31 DTEELKDILGRDIYRVREENDRMLQEVRASHEHYKKRQKQLFTGIGAMLLVFMLFALIMTIGSDFMSFLHVDILQKAIAS 110
Cdd:pfam03904   1 EAPDVADTFKKDSYTVREETKKMLDEVNKSHEDYQKYKKIAVIGIGAMLLVFMLFALVMTIGNDFMEFLHVDHLQEAIAS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2595077938 111 KIRASEGFMTFVWYIAYGLPYILSIGLFIGLYEWIRAKFHD 151
Cdd:pfam03904  81 KMKASEGFITVLWYIAYGLPYILAIGIFIYLYEWIRRRFML 121

3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. 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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2595077938  96 MSFLHVDILqkaIASKIRASEGFMTFVWYIAYGLPYILSIGLFIGLYEWIR 146
Cdd:cd09812   209 VEFVHVDNL---VQAHILAAEALTTAKGYIASGQAYFISDGRPVNNFEFFR 256