ID A0A066VUJ8_TILAU Unreviewed; 924 AA.
AC A0A066VUJ8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Histidine biosynthesis trifunctional protein {ECO:0000256|ARBA:ARBA00017884};
DE EC=1.1.1.23 {ECO:0000256|ARBA:ARBA00012965};
DE EC=3.5.4.19 {ECO:0000256|ARBA:ARBA00012721};
DE EC=3.6.1.31 {ECO:0000256|ARBA:ARBA00012414};
GN ORFNames=K437DRAFT_248094 {ECO:0000313|EMBL:KDN43943.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN43943.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN43943.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN43943.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-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 -!- 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 -!- 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 -!- 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 -!- 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:KDN43943.1}.
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DR EMBL; JMSN01000056; KDN43943.1; -; Genomic_DNA.
DR RefSeq; XP_013242564.1; XM_013387110.1.
DR AlphaFoldDB; A0A066VUJ8; -.
DR STRING; 1037660.A0A066VUJ8; -.
DR GeneID; 25263284; -.
DR HOGENOM; CLU_006732_0_2_1; -.
DR InParanoid; A0A066VUJ8; -.
DR OMA; VFVVKQI; -.
DR OrthoDB; 50870at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000027361; Unassembled WGS sequence.
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 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000027361};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 243..319
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
SQ SEQUENCE 924 AA; 98303 MW; 01681D835F31118F CRC64;
MSQQQLSVPL LPVLEGGVLP SPTELAIFAR SVPLVIPFAA LKSAFSQLKP KGGNGSTRQQ
AYIVSLDETS TESAASDILN DGAEVVFTPN GDLLEHGLPA ERVVLSISPD TALPLSDFLE
KHSDLAGLHV TLPAGLQASS AQAGELLASY SKLLDTKKTG KALFVSLSAG QTASVEDVKL
LASTYSASLL VASTLLSFSE NVDQTPSDKL DFATAFFSPL GSDRTDGLFP TIVTSTLGQS
LGLVYSSQAS LRASLLSGCG TYQSRNRGLW QKGLTSGATQ HVRQIRFDCD FDAIEFRVTQ
NAGKNGESFC HLPVRDSCFG PLTGLERLQH TIQQRKRNAP AGSYTARLFS DEQLLGAKIR
EEAQELIDAK DVDKEHVAFE MADLMYFAFV RCAKAGVTLE DVEEALEGKA KKVQRRKGDA
KPAFVNGGSA ATVATAAQAA PASTEQGSTP APSDDIKMAS YRLSDLSPQQ KIDLLKRPSI
KSGAIMDIAR PILSAVRERG DAALLEYTAK FDRCSCLKSP VRFPPFVDDE VMRKIKPEVK
NAIDVAYRNI HAFHKAQKAT TGNKKAEEAG CQAAGITGAF EDAEDAVLEM ETQPGVVCRR
FARPIQRVGL YVPGGTAVLP STALMLGVPA KVAKCPTIVL ATPPRQDGSI APEVLYVASL
VGATCILAAG GAQAVAAMAY GTETVPKVDK IVGPGNQFVT AAKMIVQNET DTLVSIDMPA
GPSEVLVIAD ASADPAFVAS DLLSQAEHGP DSQVVLVAIA LNESQLKAIE RELDTQAKRL
PRVGTVRKAI EKSVTIVVND RKQAIDWSNA YAPEHLILQV EDAEEMVKSV ENAGSVFVGM
WSPESCGDYA SGTNHTLPTY GFARQYSGVS TSTFEKHITS QSLTSEGLQG LGPHVVHLAE
CEGLEAHAQA VRVRLQALQK RATA
//
