ID HISX_BACSU STANDARD; PRT; 427 AA. AC O34651; DT 15-JUL-1998 (REL. 36, CREATED) DT 15-JUL-1998 (REL. 36, LAST SEQUENCE UPDATE) DT 15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE) DE HISTIDINOL DEHYDROGENASE (EC 1.1.1.23) (HDH). GN HISD. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RA LAZAREVIC V., SOLDO B., RIVOLTA C., REYNOLDS S., MAUEL C., RA KARAMATA D.; RL SUBMITTED (AUG-1997) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: THIS PROTEIN IS CONSIDERED AS A BIFUNCTIONAL ENZYME, CC POSSESSING TWO ACTIVE SITES, ONE AN ALCOHOL DEHYDROGENASE AND CC THE OTHER AN ALDEHYDE DEHYDROGENASE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: L-HISTIDINOL + 2 NAD(+) = L-HISTIDINE + CC 2 NADH. CC -!- PATHWAY: TENTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: TO OTHER PROKARYOTIC, FUNGAL AND PLANTS HDH. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF017113; G2618866; -. DR EMBL; Z99121; E1186179; -. DR SUBTILIST; BG12599; HISD. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. KW HISTIDINE BIOSYNTHESIS; MULTIFUNCTIONAL ENZYME; OXIDOREDUCTASE; NAD. SQ SEQUENCE 427 AA; 46256 MW; 79D62A53 CRC32; MKIKTISGAE RLSLKRSIDA GTEEQRKTVR SIIEDVKANG DQAVRSYTAK FDCIEIDSPL VTKEEFEEAY TSLDSRLLQV IRQAIENIRE YHERQLQSSW FYHRKDGTML GQKVTALDSA GVYVPGGTAA YPSSVLMNVI PALVAGVERI VLVTPPGKDG LLSPGVLVAA AELGIKDIYK MGGAQAIAAL AYGTETIEPV DKITGPGNIY VALAKREVFG DVDIDMIAGP SEIVVLADET AIPSEIAADL LSQAEHDKLS SCVFVTDSMA LAETVSAEVN KQLETLPRRE IAEASVRDYG CIYVAETMVE AIETVNTLAP EHLEIITQSP EALLGSIKHA GAIFLGRYSP EPVGDYFAGP NHVLPTNGTA RFSSPLNVTD FQKKSSIISY SQSAFEEHAE SIAAFARLEG LEAHARSIEA RERRISK //