HIS2_KLULA
ID HIS2_KLULA Reviewed; 795 AA.
AC O13471; Q6CUX9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Histidine biosynthesis trifunctional protein;
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE EC=3.5.4.19;
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase;
DE EC=3.6.1.31;
DE Includes:
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=HIS4; OrderedLocusNames=KLLA0C01452g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=9639316;
RX DOI=10.1002/(sici)1097-0061(199805)14:7<687::aid-yea261>3.0.co;2-4;
RA Freire-Picos M.A., Hampsey M., Cerdan M.E.;
RT "The HIS4 gene from the yeast Kluyveromyces lactis.";
RL Yeast 14:687-691(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
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. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; Y09503; CAA70698.1; -; Genomic_DNA.
DR EMBL; CR382123; CAH01111.1; -; Genomic_DNA.
DR RefSeq; XP_452260.1; XM_452260.1.
DR AlphaFoldDB; O13471; -.
DR SMR; O13471; -.
DR STRING; 28985.XP_452260.1; -.
DR EnsemblFungi; CAH01111; CAH01111; KLLA0_C01452g.
DR GeneID; 2892606; -.
DR KEGG; kla:KLLA0_C01452g; -.
DR eggNOG; KOG2697; Eukaryota.
DR eggNOG; KOG4311; Eukaryota.
DR HOGENOM; CLU_006732_0_0_1; -.
DR InParanoid; O13471; -.
DR OMA; WEAADLF; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06572; Histidinol_dh; 1.
DR Gene3D; 3.10.20.810; -; 1.
DR HAMAP; MF_01024; HisD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR016298; Histidine_synth_trifunct.
DR InterPro; IPR001692; Histidinol_DH_CS.
DR InterPro; IPR012131; Hstdl_DH.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR PIRSF; PIRSF001257; His_trifunctional; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF141734; SSF141734; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Histidine biosynthesis; Hydrolase;
KW Metal-binding; Multifunctional enzyme; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..795
FT /note="Histidine biosynthesis trifunctional protein"
FT /id="PRO_0000135910"
FT REGION 1..225
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 226..308
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT REGION 309..795
FT /note="Histidinol dehydrogenase"
FT ACT_SITE 683
FT /evidence="ECO:0000250"
FT ACT_SITE 684
FT /evidence="ECO:0000250"
FT BINDING 614
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 617
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 717
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 776
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 162..163
FT /note="VY -> DI (in Ref. 1; CAA70698)"
FT /evidence="ECO:0000305"
FT CONFLICT 580..582
FT /note="QAL -> LAI (in Ref. 1; CAA70698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 86795 MW; 6D35F1632280D3B3 CRC64;
MLPVVPVFNA VNALKEKTYL YLSSQLVLDG KDMTKDDILE FVQNSHGQNI SVLLKDAKFE
DDDLIVLLNN GVVTLFIDSD DYAAHLVEIG VPSIRLTLLK DGAYQFSFGQ IQEIQQSQLV
KASEISLETF TNSVLSGMKT DRPDGLYTTL VVDENERSLG LVYSNKESVS LAIETQTGIY
FSRSRNEIWR KGATSGNVQK LLSIELDCDG DALKFVVRQG GSGSFCHLET ESCFGNFRHG
LYGLQKLLQE RLLNAPEGSY TKRLFNDSDL LTAKIKEEAE ELTEAVDKKD IAWECADLFY
FAMARLVANG VSLEDVERNL NTKHLKITRR KGDAKPKFLK KEPVAVHEED GKIVLNVVSA
SDKAAVEKAV TRPIQKTAEI MNLVNPIIEN VIKNGDKALV ELTAKFDGVQ LETPVLEAPY
PEEYLDGLTD ELRDALDLSI ENVKKFHAAQ MQSETLDVET QPGVVCSRFP RPIEKVGLYI
PGGTAILPST ALMLGVPAQV AGCKEIVFAS PPRKSDGRVS PEVVYVASKV GASKIVLAGG
AQAIAAMAYG TESVPKVDKI LGPGNQFVTA AKMYVQNDTQ ALCSIDMPAG PSEVLVICDE
EADVDFVASD LLSQAEHGID SQVILVGVSL SDSKIEALQN AVHEQAMQLP RVDIVRKCIA
HSSIILCDSY EEAFKMSNQY APEHLILQIS NAEDYVKDVD HAGSIFVGAY TPESCGDYSS
GTNHTLPTYG YARQYSGVNT ATFQKFITSQ VVTPVGLEHI GHAVMSVAKV EGLDAHRNAV
KIRMSKLGLL PSGFE
