(S)-mandelate dehydrogenase

Name	(S)-mandelate dehydrogenase
Synonyms	1.1.99.31 L(+)-mandelate dehydrogenase MDH
Gene Name	mdlB
Organism	Pseudomonas putida
Amino acid sequence	>lcl\|BSEQ0019362\|(S)-mandelate dehydrogenase MSQNLFNVEDYRKLRQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRR SLQAEVLGKRQSMPLLIGPTGLNGALWPKGDLALARAATKAGIPFVLSTASNMSIEDLAR QCDGDLWFQLYVIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRERDLHNRFKIPMSYS AKVVLDGCLHPRWSLDFVRHGMPQLANFVSSQTSSLEMQAALMSRQMDASFNWEALRWLR DLWPHKLLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGKPV LIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIG CPDITSLSPDYLQNEGVTNTAPVDHLIGKGTHA
Number of residues	None
Molecular Weight	43436.53
Theoretical pI	8.22
GO Classification	Functions FMN binding (S)-mandelate dehydrogenase activity Processes mandelate catabolic process Components membrane
General Function	Fmn binding
Specific Function	Reduction of (S)-mandelate to benzoylformate.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P20932
UniProtKB Entry Name
Cellular Location	Membrane
Gene sequence	>lcl\|BSEQ0005915\|1182 bp TCATGCGTGTGTTCCTTTACCAATGAGGTGATCGACTGGAGCGGTGTTAGTCACTCCCTC GTTTTGGAGGTAATCAGGAGAAAGGGAGGTGATGTCAGGGCATCCAATCTGGGCAAGGGT GCGGTCGATATCCGCTTTTAGGAGGGTTAGCACCTCGTCAACACCCGTTTCACCTCGTGC TGCAAGGCCATACAAAGTTGCACGACCCAGGAGTACAGCCTCAGCACCTAGCGCAAGTGC TTTAACGATGTCCGAACCCCGTCGGAAGCCGCTATCGATAAGCACTGGTTTTCCAGTTTT CGCTACCGATTGAGCCAAAACTTCCATTGGCGATATCGCGCAATCGAGTTGGCGACCGCC GTGGTTTGATAGGATTACGCCGTCTGCACCTTCAGCGATGCACCGATCGGCGTCCTCAGC ACTGAGCAACCCCTTTACGAGGAGTTTGTGCGGCCAGAGGTCACGCAGCCATCTCAATGC CTCCCAGTTGAAACTGGCATCCATTTGGCGGCTCATCAATGCTGCCTGCATTTCTAAGCT AGACGTTTGACTGCTGACGAAATTGGCCAGTTGCGGCATGCCGTGTCGCACGAAGTCGAG CGACCAGCGCGGATGCAGGCATCCGTCCAGCACCACCTTTGCGGAGTAGCTCATTGGTAT CTTGAATCGGTTATGCAGGTCGCGCTCGCGATAGCCGTTAACCGCCACATCCGTAGTAAG CACCAGTGTCGTGTAACCAGTGTGCAGGGCTTTGAGCACCATCCCCTGCGCAATCTCTCG GTGGATCACATAGAGCTGGAACCACAGATCGCCATCACACTGACGTGCGAGGTCTTCAAT GGACATGTTGGAGGCGGTCGACAGCACGAACGGGATTCCGGCCTTGGTTGCTGCTCGAGC TAAAGCGAGATCCCCCTTAGGCCACAGCGCACCGTTCAGCCCAGTAGGCCCAATCAAGAG AGGCATCGACTGCCTCTTTCCAAGTACTTCCGCTTGGAGGCTGCGGCGGCTGACGTCTAC TAGCCGCTTCGGTTTGAATCGCCATTGCTGGAAGACGTCGCGGTTGTGTTTCACCCCGTA TTCGTCTTCAGCCCCACCTTCCAGATAGTCGTAGACCATCTTCGGCAAGCGCTTTTGCCG AAGCTTGCGATAGTCCTCAACGTTAAAGAGATTCTGGCTCAT
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Tsou AY, Ransom SC, Gerlt JA, Buechter DD, Babbitt PC, Kenyon GL: Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry. 1990 Oct 23;29(42):9856-62. [2271624 ] Sukumar N, Xu Y, Gatti DL, Mitra B, Mathews FS: Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase. Biochemistry. 2001 Aug 21;40(33):9870-8. [11502180 ] Sukumar N, Dewanti AR, Mitra B, Mathews FS: High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase. J Biol Chem. 2004 Jan 30;279(5):3749-57. Epub 2003 Nov 6. [14604988 ]

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