ID A0A066XQR6_COLSU Unreviewed; 866 AA.
AC A0A066XQR6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 41.
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=CSUB01_06792 {ECO:0000313|EMBL:KDN68335.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN68335.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN68335.1}.
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DR EMBL; JMSE01000680; KDN68335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XQR6; -.
DR STRING; 1173701.A0A066XQR6; -.
DR eggNOG; KOG2697; Eukaryota.
DR eggNOG; KOG4311; Eukaryota.
DR HOGENOM; CLU_006732_0_0_1; -.
DR OMA; VFVVKQI; -.
DR OrthoDB; 50870at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000027238; 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:UP000027238};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 222..292
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT REGION 393..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 93599 MW; A955F1C856502FF3 CRC64;
METTLPFPFL VSVAVPPGLS KLDGLDREQV SILGAPFFEA NDQTLEKFHN FLKQHNAEFR
GYFDVTGISS RDDVVSLLDA GARMVFVSPE NLGQYEEFGS RVGSVLSTAD VTTKPASKHA
VLVKDFDSTI CDLGSFIERC KVEKLPNLFI KPVPESNLDH FVDIAKQCNA IPVLPSDGLT
ASEEEPNKLS LSKLISSFWK SDRPDGLIPT VVCDESGTAL GLAYSSAESV GEALRTRTGV
YQSRKRGLWV KGATSGDTQD LVRIALDCDN DTLKFVVRQK GGFCHLDQHG CFGDLNGIPR
LEQTLQSRKK SAPAGSYTAR LFSDEKLLRA KIMEEAEELC DAKTPQDVAF EAADLIYFAL
TKAVSAGVSL ADIEKNLDAK SFKVKRRTGD AKGKWAEKEG IKSSSAPSPT VAPAQAPASK
DEKSNRITMR RYDLTKSSAA EIDEVLKRPS QKSPDAILNI VKPIIDEVRN GGDKAVLSYT
HKFEKATSLT SPVLKAPFPK EAMQLSPEST KAIDISFENI RKFHAAQKED KPLQVETMPG
VVCSRFSRPI ERVGLYVPGG TAVLPSTALM LGVPAMVAGC QKIVIASPPR ADGSLTPEIV
YVAHKIGAES IVLAGGAQAV AAMAYGTESV TKVDKILGPG NQFVTAAKMF VSNDTNAGVS
IDMPAGPSEV LVIADKDANP AFVASDLLSQ AEHGVDSQVV LIAIDLTEQQ LQAIEDELHS
QAMALPRVDI VRGSIAHSVT IQVKTVDEAM RISNDYAPEH LILQVKDAEK VTEKVMNAGS
VFIGEWTPES VGDYSAGVNH SLPTYGYAKQ YSGVNLASFV KHITSSNLTA EGLRNVGEAV
MQLAKTEQLE AHRRAVEIRI DHMNRK
//
