ID   HIS8_PHOLL              Reviewed;         807 AA.
AC   Q7N6I1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Putative histidine biosynthesis bifunctional protein HisCD;
DE   Includes:
DE     RecName: Full=Histidinol dehydrogenase;
DE              Short=HDH;
DE              EC=1.1.1.23;
DE   Includes:
DE     RecName: Full=Histidinol-phosphate aminotransferase;
DE              EC=2.6.1.9;
DE     AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisCD; Synonyms=hisD; OrderedLocusNames=plu1569;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01) (Photorhabdus luminescens subsp. laumondii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC         oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC         ChEBI:CHEBI:57980; EC=2.6.1.9;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC         Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC         ChEBI:CHEBI:57945; EC=1.1.1.23;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the histidinol
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC       pyridoxal-phosphate-dependent aminotransferase family. Histidinol-
CC       phosphate aminotransferase subfamily. {ECO:0000305}.
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DR   EMBL; BX571864; CAE13862.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7N6I1; -.
DR   SMR; Q7N6I1; -.
DR   STRING; 243265.plu1569; -.
DR   KEGG; plu:plu1569; -.
DR   eggNOG; COG0079; Bacteria.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_011806_0_0_6; -.
DR   UniPathway; UPA00031; UER00012.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00609; AAT_like; 1.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   Gene3D; 1.20.5.1300; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   HAMAP; MF_01024; HisD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01141; hisC; 1.
DR   NCBIfam; TIGR00069; hisD; 1.
DR   PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN           1..807
FT                   /note="Putative histidine biosynthesis bifunctional protein
FT                   HisCD"
FT                   /id="PRO_0000153415"
FT   REGION          1..440
FT                   /note="Histidinol dehydrogenase"
FT   REGION          441..807
FT                   /note="Histidinol-phosphate aminotransferase"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         421
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         655
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   807 AA;  88850 MW;  648F98DD2F9F706E CRC64;
     MTDHFDTLIR WQECHDEQQN ALLTRPAISA SVEISRTVEQ ILHAVKEYGD HTLREFSRRF
     DKTVIENIRI SPEEIAAAEN SLNNDIKQAM QQAMNNIRVF HEAQKPIKIE VETQPGVYCQ
     QVTRPIDSVG LYIPGGSAPL LSTVLMLGTP AQIAGCHKVV LCSPPPIANE ILYAATLCGI
     TEIFQIGGAQ AIAAMAFGTE SVPKVDKIFG PGNAYVTEAK RQVSQRVDGA TIDMPAGPSE
     LLIIADAGAN PVFVAADLLS QAEHGPDSQV ILVTPDEALA KKVITEIEKQ LTRLPRNQIA
     AKALAHSRII VTTSLQQCVE ISNRYGPEHL IIQTRQPEQL VEKITSAGSV FLGDWSPESA
     GDYASGTNHV LPTYGYTSTY SSLGLADFLK RMTIQQLTPQ GLLNLSQTIE TLAQAEQLTA
     HKNALTLRVA ALNIAGQGVN MNNIFDANLL ARENIRKLTP YMSARRLGGK GDVWLNANEY
     PLAPDFQCTE QTLNRYPDCQ PASVIRRYAA YAGLQPEQVL ACRGADESIE LLIRVFCEPG
     QDVVLFCPPT YGMYSVSAET FGVEQKKITA LENWQLDIEA IENNLDRVKL IYICSPNNPT
     GNAINPDSLR KILELTANRA IVTIDEAYIE FCPENSIASW LKNYPNLVIL RTLSKAFALA
     GLRCGFTLAS VDIITLLLKV IAPYPLSTPV ADIAAQALTA ENIAIMQKRV VEIRENRNDL
     QQALNKLAIV EKVFPSETNY ILVKFYDAET VFKTLWHQGI ILRDQRKQPG LEGCLRITIG
     SRKECERVVE AISALSTVNE QPKEIAN
//