ID A0A1B8EUJ8_9PEZI Unreviewed; 859 AA.
AC A0A1B8EUJ8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
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=VF21_06356 {ECO:0000313|EMBL:OBT75023.1};
OS Pseudogymnoascus sp. 05NY08.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT75023.1, ECO:0000313|Proteomes:UP000092096};
RN [1] {ECO:0000313|EMBL:OBT75023.1, ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|EMBL:OBT75023.1,
RC ECO:0000313|Proteomes:UP000092096};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV458835; OBT75023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8EUJ8; -.
DR STRING; 1622149.A0A1B8EUJ8; -.
DR OrthoDB; 50870at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000092096; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092096};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 217..288
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
SQ SEQUENCE 859 AA; 91994 MW; B1CAEB3D5276F5E7 CRC64;
METTIPLPLV PSLDLASQPY FETGLPRKQL SHLGSIFFVA KNETFDLVFG FLQGHTAVRT
FVNAAALQES DILSLLDAGA RCVFVKEEQA ASLEKYGDRI GLVATSAASK VPAGGALIDF
GGDAAASKAL LKTFVDQKTS PVFLVTPEES KAQETVTIAQ ELGVVPIVPA TALTMENKDT
DGKLSVPAII GSQWASDRAD KLIPTVVTDE RGVALGLVYS SQESISESLK TSTGVYQSRK
RGLWYKGASS GDTQELVRLS LDCDQDCLKF VVRQKGRGFC HLPQPTCFGE LGGISKLEKT
LQSRKISAPE GSYTARLFSD EKLLRAKIME EAEELCDAKT KEEIAFEAAD LIYFALTKAV
AAGVTLADIE TSLDAKSVKV KRRQGDAKGQ WAAKEGIAVA PKEAAKAPTV VKKEDGPILM
KRYDASQISE KELLDVLQRP SQKSNEMIMG IVNPIITAVR TRGDAAVLEY THKFEKATSL
TSPILRAPFP QSMMNLPQET IDAIDISFEN IRKFHAAQKE DKPLEVETMP GIICSRFVRP
IERVGLYVPG GTAVLPSTAL MLGVPAMVAG CKRIVMATPP RADGSITPEV IYAAHKVGAE
CIVLAGGAQA VAAMAYGTES VPKVDKILGP GNQFVTAAKM HVSNDTNAGV SIDMPAGPSE
VLVVADKSAN PAFVASDLLS QAEHGVDSQV ILIAIDLSET ELKAIEDALH EQAIALPRVD
IVRGAIAHSV TLVVKSLEEA MRLSNDYAPE HLILQIKDAA AAVDLVENAG SVFVGEWTPE
SVGDYSAGVN HSLPTYGYAK QYSGVNLGSY VKHITSSNLT AQGLRNVGGA VMQLAKVEEL
EAHRRAVGIR LKWMDERGL
//
