HIS8_PHOLL
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 03-AUG-2022, entry version 119.
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).
OC Bacteria; Proteobacteria; 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 EnsemblBacteria; CAE13862; CAE13862; plu1569.
DR KEGG; plu:plu1569; -.
DR eggNOG; COG0079; Bacteria.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_011806_0_0_6; -.
DR OrthoDB; 935289at2; -.
DR BioCyc; PLUM243265:PLU_RS25180-MON; -.
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; cd06572; Histidinol_dh; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR TIGRFAMs; TIGR00069; hisD; 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
