(data stored in ACNUC30567 zone)

HOGENOM: ACAM1_1_PE2812

ID   ACAM1_1_PE2812                       STANDARD;      PRT;   435 AA.
AC   ACAM1_1_PE2812; B0CBB6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Histidinol dehydrogenase; Short=HDH; EC=1.1.1 23;
DE   (ACAM1_1.PE2812).
GN   Name=hisD; OrderedLocusNames=AM1_2902;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE2812.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:B0CBB6_ACAM1
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine
CC       + 2 NADH.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC   -!- GENE_FAMILY: HOG000243914 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0CBB6; -.
DR   EMBL; CP000828; ABW27901.1; -; Genomic_DNA.
DR   RefSeq; YP_001517217.1; NC_009925.1.
DR   ProteinModelPortal; B0CBB6; -.
DR   STRING; B0CBB6; -.
DR   GeneID; 5681710; -.
DR   GenomeReviews; CP000828_GR; AM1_2902.
DR   KEGG; amr:AM1_2902; -.
DR   OMA; KIVGPGS; -.
DR   ProtClustDB; PRK00877; -.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01024; HisD; 1; -.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR022695; Histidinol_DH_monofunct.
DR   InterPro; IPR012131; Hstdl_DH.
DR   PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PIRSF; PIRSF000099; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   TIGRFAMs; TIGR00069; HisD; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
DR   HOGENOMDNA; ACAM1_1.PE2812; -.
KW   histidinol dehydrogenase;
KW   Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
SQ   SEQUENCE   435 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVRILRLSEM TSEELASIKR RAELDIEQAL AVAKEVIDEI RADGDQGVIK YVRKFDFPGA
     TAENLKVTEA EFAAAREQVE PEIKAAIEQA YRNIKEVHER QMPEEVQLAE IDGGVFAGEK
     VTPIASAGLY VPRGKGSFPS VMLMLSVPAV VAGVEKVVVC TPPDKNGTVE PASLVAAELA
     GVKDIYKLGG IQAIAGMAIG TETVPKVDKI TGPCNVYGSA AKRLLYGTVD VGLPAGPSES
     IILTDETTDP RIAALDLLVE AEHGPDSAGL LVTHSEDLAK AASKHADDYM EKLPDWRKNF
     CQTGLSSYGG IILTSSLEES IDFLNEYAPE HLEVLVQDPL SVLGKIKNAG EILLGPYTPI
     PTANYCIGVN AILPTGGFAR SYSAVSVYDF LKRTGIGYLT QEGFARLGHT AQTLAEHEDF
     PAHAMAIRER KNLLP
//

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