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LOCUS WP_003104350 497 aa linear BCT 25-JUL-2024 dehydrogenase [Pseudomonas]. ACCESSION WP_003104350 VERSION WP_003104350.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 497) AUTHORS Stines-Chaumeil,C., Talfournier,F. and Branlant,G. TITLE Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis JOURNAL Biochem J 395 (1), 107-115 (2006) PUBMED 16332250 REFERENCE 2 (residues 1 to 497) AUTHORS Yoshida,K.I., Aoyama,D., Ishio,I., Shibayama,T. and Fujita,Y. TITLE Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis JOURNAL J Bacteriol 179 (14), 4591-4598 (1997) PUBMED 9226270 REFERENCE 3 (residues 1 to 497) AUTHORS Zhang,Y.X., Tang,L. and Hutchinson,C.R. TITLE Cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces coelicolor JOURNAL J Bacteriol 178 (2), 490-495 (1996) PUBMED 8550471 REFERENCE 4 (residues 1 to 497) AUTHORS Kedishvili,N.Y., Popov,K.M., Rougraff,P.M., Zhao,Y., Crabb,D.W. and Harris,R.A. TITLE CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution JOURNAL J Biol Chem 267 (27), 19724-19729 (1992) PUBMED 1527093 REFERENCE 5 (residues 1 to 497) AUTHORS Steele,M.I., Lorenz,D., Hatter,K., Park,A. and Sokatch,J.R. TITLE Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase JOURNAL J Biol Chem 267 (19), 13585-13592 (1992) PUBMED 1339433 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR01722.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..497 /organism="Pseudomonas" /db_xref="taxon:286" gene 1..497 /gene="mmsA" Protein 1..497 /product="CoA-acylating methylmalonate-semialdehyde dehydrogenase" /EC_number="1.2.1.27" /GO_function="GO:0004491 - methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity [Evidence IEA]" /calculated_mol_wt=53532 Region 5..481 /region_name="MMSDH" /note="methylmalonic acid semialdehyde dehydrogenase; TIGR01722" /db_xref="CDD:130783" Site order(62,64,68,71,75,108,111..112,121..128,133,136,139, 232,236,239,242,244,417,419..420,422..423,426,429..430, 432,434..437,446,450,452,466,473..478,480..481) /site_type="other" /note="tetrameric interface [polypeptide binding]" /db_xref="CDD:143404" Site order(148..151,159,174,177,207,224..227,230,248..250,282, 382,384,410) /site_type="other" /note="NAD binding site [chemical binding]" /db_xref="CDD:143404" Site order(151,248,279,282) /site_type="active" /note="catalytic residues [active]" /db_xref="CDD:143404" ORIGIN 1 msvpvrhlia gafveglgaq ripvsnpldn stlaeiacas aeqveqavas aretfaswke 61 tpvserarvm lryqallkeh hdelakivss elgktfedak gdvwrgievv ehacnvpsll 121 mgetvenvar nidtysitqp lgvcvgitpf nfpamiplwm fplaiacgna filkpseqvp 181 ltsvrlaelf leagapkgvl qvvhggkeqv dqllkhpqvk avsfvgsvav gqyvyhtgta 241 hnkrvqsfag aknhmvimpd adkaqvisnl vgasvgaagq rcmaisvavl vgaarewipe 301 irdalakvrp gpwddsgasy gpvinpqaka rierligqgv eegaqllldg rgykvegypd 361 gnwvgptlfa gvrpdmaiyr eevfgpvlcl aevdsleqai rlinespygn gtsiftssga 421 aartfqhhie vgqvginipi pvplpffsft gwkgsfygdl haygkqgvrf ytetktvtar 481 wfdsdsvagt nfsiqmr