ID A0A9P6EWY6_9FUNG Unreviewed; 877 AA. AC A0A9P6EWY6; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 08-NOV-2023, entry version 2. 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 Name=HIS4 {ECO:0000313|EMBL:KAF9537340.1}; GN ORFNames=EC957_008414 {ECO:0000313|EMBL:KAF9537340.1}; OS Mortierella hygrophila. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina; OC Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella. OX NCBI_TaxID=979708 {ECO:0000313|EMBL:KAF9537340.1, ECO:0000313|Proteomes:UP000723463}; RN [1] {ECO:0000313|EMBL:KAF9537340.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 2591 {ECO:0000313|EMBL:KAF9537340.1}; RX PubMed=33364917; RA Vandepol N., Liber J., Desiro A., Na H., Kennedy M., Barry K., RA Grigoriev I.V., Miller A.N., O'Donnell K., Stajich J.E., Bonito G.; RT "Resolving the Mortierellaceae phylogeny through synthesis of multi-gene RT phylogenetics and phylogenomics."; RL Fungal Divers. 104:267-289(2020). 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAF9537340.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAAAXW010000418; KAF9537340.1; -; Genomic_DNA. DR Proteomes; UP000723463; Unassembled WGS sequence. 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; 1. 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|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}; Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 233..304 FT /note="Phosphoribosyl-AMP cyclohydrolase" FT /evidence="ECO:0000259|Pfam:PF01502" SQ SEQUENCE 877 AA; 94272 MW; 4CD9481BD9364182 CRC64; MIIPRIDIAA DSYKDDLTAF SALPNQVLVV PTPDNDRLND ILKNQHKDAY WIQPLAFDPQ DPLAQIHTLL DAGADKVVLP YAAFANADLE SSFSHIPQER LAVTLTPAEF AHLDRLLATV SVFILELTDT SAESLEAIKA AAQLALKDLL PRGGVKRVVA SFASSTATPG LLAISELGRL GVDTQLSTNI LSTGHEDGKL NLGEAFMATV VSDRPDGLFP TIVVDEQGIS LGLVYSSLES VVESFRTGKG VYFSRTRGLW HKGASSGSTQ DLVKAHVDCD SDALQFTVHQ HGTGFCHNNI RGCFGPSSGL AHLDQTLKSR KISAPAGSYT QRLFKDSNLV QSKIMEEAEE LCEAKTPQDI AWETADLFYF ALVKCIANGV SLRDVEQQLE NRSRKITRRP GHAKPKWDVS AKEAAAAAAA AAAAPVAPAP ASENGKSGRI SMKSYKMNAL SAEQQSKLLL RPIIQSNDIM ARVKPIVEGV RERGDAALIE FTAKFDGVQL ESTVISAPFS PESMILDEKT RAAIDQAYDN IHKFHAAQLQ DKALVVETMP GVVCTRFARP IERVGLYVPG GTAVLPSTAL MLGIPAAVAG CSEIVIATPP RKDGSIVPEV MYVAHKVGAS KVLMAGGAQA VAAMAYGTES CPKVDKICGP GNQYVTAAKM LTQIDSSSLV SIDMPAGPSE LLVIADMTSI PAYVASDLLS QAEHGTDSQV VLIAVGLTAE HLAAIEDEVH DQASRLPRVD IVRESIPKSY IIDVESMEEA MRFSNAYAPE HLILHLEEAE KHVDQVMNAG SVFVGHWSPE SCGDYASGTN HTLPTYGYAR MYSGVNTDTF LKHITSQQLT REGLDAIGDT VMRLAEIEGL EAHRNAVGVR IRDIRGL //