ID A0A0C7NF19_9SACH Unreviewed; 809 AA.
AC A0A0C7NF19;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=Histidine biosynthesis trifunctional protein {ECO:0000256|PIRNR:PIRNR001257};
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|PIRNR:PIRNR001257};
DE EC=3.5.4.19 {ECO:0000256|PIRNR:PIRNR001257};
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase {ECO:0000256|PIRNR:PIRNR001257};
DE EC=3.6.1.31 {ECO:0000256|PIRNR:PIRNR001257};
DE Includes:
DE RecName: Full=Histidinol dehydrogenase {ECO:0000256|PIRNR:PIRNR001257};
DE Short=HDH {ECO:0000256|PIRNR:PIRNR001257};
DE EC=1.1.1.23 {ECO:0000256|PIRNR:PIRNR001257};
GN ORFNames=LALA0_S11e01178g {ECO:0000313|EMBL:CEP64308.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64308.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP64308.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64308.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000024,
CC ECO:0000256|PIRNR:PIRNR001257};
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 Evidence={ECO:0000256|ARBA:ARBA00001460,
CC ECO:0000256|PIRNR:PIRNR001257};
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 Evidence={ECO:0000256|ARBA:ARBA00001654,
CC ECO:0000256|PIRNR:PIRNR001257};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000256|ARBA:ARBA00005204}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000256|ARBA:ARBA00005169}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC {ECO:0000256|ARBA:ARBA00004940}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00008260,
CC ECO:0000256|PIRNR:PIRNR001257}.
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DR EMBL; LN736370; CEP64308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7NF19; -.
DR STRING; 1245769.A0A0C7NF19; -.
DR HOGENOM; CLU_006732_0_0_1; -.
DR OrthoDB; 50870at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000054304; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06572; Histidinol_dh; 1.
DR CDD; cd11546; NTP-PPase_His4; 1.
DR Gene3D; 1.20.5.1300; -; 1.
DR Gene3D; 1.10.287.1080; MazG-like; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 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 NCBIfam; TIGR00069; hisD; 1.
DR NCBIfam; TIGR03188; histidine_hisI; 1.
DR PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR PIRSF; PIRSF001257; His_trifunctional; 2.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR SUPFAM; SSF141734; HisI-like; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR001257};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001257};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW ECO:0000256|PIRNR:PIRNR001257};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001257};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR001257};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001257};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR001257};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 168..242
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
SQ SEQUENCE 809 AA; 88719 MW; CCA580046952EAF0 CRC64;
MVFPILPFFT NGKDLRSVVE VKPFISLSGQ ALLDLSQIEI AEAAAFVEEN TAFKFVCGLL
KSDHQISDND IISFVNSGIA VLFVANETEA TRLQDLGIPK ERVAVDSGSA YASRFEVVQD
FQKDLIIDAG SLTETQMAQS LISTLRTDRA DKLYTTLVVD SYERCLGLVY SSEESIKLAI
QKQVGIYYSR SRNEIWEKGL TSGNTQKLVN IRLDCDGDAL KFVVVQEGKK SDFCHLNTAS
CYGEFQSGLV GLEQLLRQRF ENAPEKSYTR RLFNDPDLLT AKIKEEAEEL TEANTKSEIS
WEAADLFYFA MVKLVASGVS LEAVERNLHI KHLKVTRRQG DAKAKFIKQE TKPQPAQETE
SSLSGLINLA VVSGKDKKGV EAALERPIQR TSEIMHLVNP IVEKVKSEGN KALIEFTNKF
DGVKLENPVL EAPFPEEYLE GLTQEMRDAL DLSIENVRKF HDAQLQKEVL QVETQPGVLC
SRFPRPIEKV GLYIPGGTAV LPSTALMLGV PARVAQCKEI VFASPPRKSD GRVSPEVVYV
AQKVGASKIV LAGGAQAVAA MAYGTETIPK VDKILGPGNQ FVTAAKMYVQ NDTQALCSID
MPAGPSEVLV VADEHADADF VASDLLSQAE HGIDSQVILV GVSLSEQKIA EIQNALHEQA
LKLPRVDIVR KCIAHSSAVL CDSYEEAFDM SNDYAPEHLI LQIKDAADYV PLVFNAGSVF
VGAYTPESCG DYSSGTNHTL PTYGYARQYS GVNTGTFQKF ITAQSVTPEG LENIGRAVMT
VAKVEGLDAH RNAIKIRMQK LGQLPENFQ
//
