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LOCUS NP_464095 427 aa linear CON 28-AUG-2016 ACCESSION NP_464095 VERSION NP_464095.1 DBLINK BioProject: PRJNA61583 Assembly: GCF_000196035.1 DBSOURCE REFSEQ: accession NC_003210.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes EGD-e ORGANISM Listeria monocytogenes EGD-e Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 427) AUTHORS Toledo-Arana,A., Dussurget,O., Nikitas,G., Sesto,N., Guet-Revillet,H., Balestrino,D., Loh,E., Gripenland,J., Tiensuu,T., Vaitkevicius,K., Barthelemy,M., Vergassola,M., Nahori,M.A., Soubigou,G., Regnault,B., Coppee,J.Y., Lecuit,M., Johansson,J. and Cossart,P. TITLE The Listeria transcriptional landscape from saprophytism to virulence JOURNAL Nature 459 (7249), 950-956 (2009) PUBMED 19448609 REFERENCE 2 (residues 1 to 427) AUTHORS Chatterjee,S.S., Hossain,H., Otten,S., Kuenne,C., Kuchmina,K., Machata,S., Domann,E., Chakraborty,T. and Hain,T. TITLE Intracellular gene expression profile of Listeria monocytogenes JOURNAL Infect. Immun. 74 (2), 1323-1338 (2006) PUBMED 16428782 REFERENCE 3 (residues 1 to 427) AUTHORS Glaser,P., Frangeul,L., Buchrieser,C., Amend,A., Baquero,F., Berche,P., Bloecker,H., Brandt,P., Chakraborty,T., Charbit,A., Chetouani,F., Couve,E., de Daruvar,A., Dehoux,P., Domann,E., Dominguez-Bernal,G., Duchaud,E., Durand,L., Dussurget,O., Entian,K.-D., Fsihi,H., Garcia-Del Portillo,F., Garrido,P., Gautier,L., Goebel,W., Gomez-Lopez,N., Hain,T., Hauf,J., Jackson,D., Jones,L.-M., Karst,U., Kreft,J., Kuhn,M., Kunst,F., Kurapkat,G., Madueno,E., Maitournam,A., Mata Vicente,J., Ng,E., Nordsiek,G., Novella,S., de Pablos,B., Perez-Diaz,J.-C., Remmel,B., Rose,M., Rusniok,C., Schlueter,T., Simoes,N., Tierrez,A., Vazquez-Boland,J.-A., Voss,H., Wehland,J. and Cossart,P. TITLE Comparative genomics of Listeria species JOURNAL Science 294 (5543), 849-852 (2001) PUBMED 11679669 REFERENCE 4 (residues 1 to 427) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (08-NOV-2001) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 5 (residues 1 to 427) AUTHORS Glaser,P., Frangeul,L. and Rusniok,C. TITLE Direct Submission JOURNAL Submitted (06-JUN-2001) Glaser P., Institut Pasteur, Genomique des Microorganismes Pathogenes, 25 rue du Docteur Roux, 75724 Paris Cedex 15, FRANCE COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from CAC98646. RefSeq Category: Reference Genome FGS: First Genome sequenced MOD: Model Organism UPR: UniProt Genome Method: conceptual translation. FEATURES Location/Qualifiers source 1..427 /organism="Listeria monocytogenes EGD-e" /strain="EGD-e" /db_xref="taxon:169963" Protein 1..427 /product="histidinol dehydrogenase" /EC_number="1.1.1.23" /calculated_mol_wt=46099 Region 1..423 /region_name="hisD" /note="bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed; PRK00877" /db_xref="CDD:234853" Site order(53,125,127..128,136,157,183..184,186,207..209, 211..212,257) /site_type="other" /note="NAD binding site [chemical binding]" /db_xref="CDD:119329" Site order(78..79,82..83,85,88..89,92..93,96..97,104,106, 110..114,117,119,131..135,202,217,221,245..246,249..250, 252..254,256..257,327,332,335..336,338..346,348,350..351, 353..357,359,361,371..372,374..378,380..381,384..391, 406..407,409..415) /site_type="other" /note="dimerization interface [polypeptide binding]" /db_xref="CDD:119329" Site order(133,135,232,257,322..323,352,356..357,363,410,412, 415) /site_type="active" /note="product binding site [active]" /db_xref="CDD:119329" Site order(135,232,254,257,322..323,352,356..357,363,410,412, 415) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:119329" Site order(254,257,356,415) /site_type="other" /note="zinc binding site [ion binding]" /db_xref="CDD:119329" Site 322..323 /site_type="active" /note="catalytic residues [active]" /db_xref="CDD:119329" CDS 1..427 /gene="hisD" /locus_tag="lmo0567" /coded_by="complement(NC_003210.1:604121..605404)" /experiment="EXISTENCE:[PMID:19448609]" /note="catalyzes the oxidation of L-histidinol to L-histidinaldehyde and then to L-histidine in histidine biosynthesis; functions as a dimer" /transl_table=11 /db_xref="GeneID:985596" CONTIG join(WP_009930740.1:1..427) ORIGIN 1 mkiltgtine llnevkaenn tnnslqvese vksiiekvkk dgdqalfdft sqfdgvrlte 61 lrvqtadiqs asskvdpafl valqqakani esfhskqkqh afldsekdgv irgqlirple 121 tvgiyvpggt aaypssvlmn vlpakiagvk rivmitppae nginphvlaa aqlagvdeiy 181 qvggahgiaa lahgtesipk vdkivgpgni yvatakrevf glvdidmiag pseivvlade 241 nanpafiasd llsqaehdil arailittsk kiaeetqnei nkqlenlprk aiaqksietq 301 gkiiiaantq emfdimneia pehlevqlen pmnylnqikn agsiflgsya seplgdyfag 361 pnhvlptsgt akffsplgve dftkrsafis ytkealakek daivllakke gldahakaiq 421 irfeeen