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LOCUS WP_003112662 372 aa linear BCT 07-JUL-2024 alpha [Pseudomonas]. ACCESSION WP_003112662 VERSION WP_003112662.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 372) AUTHORS Ahmad,S., Glavas,N.A. and Bragg,P.D. TITLE A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change JOURNAL Eur J Biochem 207 (2), 733-739 (1992) PUBMED 1633824 REFERENCE 2 (residues 1 to 372) AUTHORS Tong,R.C., Glavas,N.A. and Bragg,P.D. TITLE Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes JOURNAL Biochim Biophys Acta 1080 (1), 19-28 (1991) PUBMED 1932078 REFERENCE 3 (residues 1 to 372) AUTHORS Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D. TITLE Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli JOURNAL Eur J Biochem 158 (3), 647-653 (1986) PUBMED 3525165 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 :: NF006942.0 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK09424 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..372 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..372 /product="Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha" /EC_number="7.1.1.1" /GO_process="GO:1902600 - proton transmembrane transport [Evidence IEA]" /calculated_mol_wt=38551 Region 1..365 /region_name="Rubrum_tdh" /note="Rubrum transdehydrogenase NAD-binding and catalytic domains; cd05304" /db_xref="CDD:240629" Site order(15,73,92,291,317,319) /site_type="other" /note="ligand binding site [chemical binding]" /db_xref="CDD:240629" Site order(44,124..125,134..135,138..139,142..143,145..146, 148..153,155,157..159,162,185..186,281..282,324..325,329, 332..333) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:240629" Site order(119..120,124,127,130,171..174,194..196,231,242, 259..261,268,270) /site_type="other" /note="NAD(P) binding site [chemical binding]" /db_xref="CDD:240629" Site order(121..122,124,134,177..178,185,201..202,204..207) /site_type="other" /note="trimer interface B [polypeptide binding]" /db_xref="CDD:240629" Site order(154..158,161,164,187,189) /site_type="other" /note="trimer interface A [polypeptide binding]" /db_xref="CDD:240629" ORIGIN 1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vsasqpdsay eaagatigsa 61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt 121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai 181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme 241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte 301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl 361 mcrdgqavrk ng