ID U5HA46_USTV1 Unreviewed; 912 AA.
AC U5HA46;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 13-SEP-2023, entry version 39.
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=MVLG_04081 {ECO:0000313|EMBL:KDE05586.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE05586.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE05586.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE05586.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE05586.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200}, and P1A1
RC Lamole {ECO:0000313|EMBL:KDE05586.1};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_04081T0}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR EMBL; AEIJ01000397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541684; KDE05586.1; -; Genomic_DNA.
DR AlphaFoldDB; U5HA46; -.
DR STRING; 683840.U5HA46; -.
DR EnsemblFungi; MVLG_04081T0; MVLG_04081T0; MVLG_04081.
DR HOGENOM; CLU_006732_0_2_1; -.
DR InParanoid; U5HA46; -.
DR OMA; VFVVKQI; -.
DR OrthoDB; 50870at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000017200; 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:UP000017200};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 238..316
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
SQ SEQUENCE 912 AA; 97065 MW; 8073A03DCDC6EB27 CRC64;
MSFTQIPFLP LVEATPDAAT QQTLLSAIAR IAPFLIVSSA LESTLPLLPT SAEYYVLQDQ
SLTDDEVYAL LDAGARKIIS KDLQLLGKVP ASRFVLHIEH ATAFSLNDPN VLNGISGALL
DTTTFNENSL KSFRTALDKA DSEQRRKDLF VLSMSRDTTS ILHEPASLKL MSKTVKGVSV
LPLNLLSTTL NTTAAPRAEN GKLSVTNLFT SFLRTDREDG LYPTVPVSTA SVPSSLGLVY
SSAASIANTI ISGNAVYYSR SRQGLWKKGE TSGAMQMVER IRLDCDADAL EFQVLETGPA
GEKDGFCHIP DQTSCFGLTN GLFSLEAALK NRVKDAPQGS YTVRLFAEPA LLKAKIMEEA
GELCAAESKE DIAAEAADLL YFALAKCVGA GIGLREISKV LDQRSLKVTR RKGDAKKEWV
DKLGLDGEQA KGVDGGVAAV EPAAKAATNG VPKAVNGDAP TAEKEDLRCQ TFDLAQVDTE
GKGKLLKRPL ASSADMFSLV APILDTVRKG GDDGLRSLVV KFDRCAPAED KAFPLVLKAP
FAEELMQLDP NVKSAIDQAH HNIKAFHQAQ MDKEAPTLKV ETMPGIVCSR FARPIERVGL
YVPGGTAILP STALMLATPA QVANCSLAVI ATPPRPDGSV SPEIVYIASL TGVDAIVKAG
GAHAVASMAY GTESVPKVDK IFGPGNQFVT AAKMSVSMDS EACCAIDMPA GPSEVLVIAD
KHANPVFVAS DLLSQAEHGA DSQVILLAID IDDKGLAAIE SEIKAQALAL PRVDIIRKSI
AHSLIIKCRD VEEAFNFSNA YAPEHLILQI ENASQYVDKV NNAGSVFVGA YSPESCGDYA
SGTNHTLPTA GWAKQYSGVS TLSFLKHITT QELTREGLAK LGPVVETLAA AEGLDAHKMA
VTLRLRVMQE SA
//
