HIS2_NEUCR
ID HIS2_NEUCR Reviewed; 870 AA.
AC P07685; O42788; O42789; Q7RVK0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Histidine biosynthesis trifunctional protein;
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE EC=3.5.4.19;
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase;
DE EC=3.6.1.31;
DE Includes:
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=his-3; ORFNames=5C2.120, NCU03139;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=74-OR23-1VA / FGSC 2489;
RX PubMed=3005109; DOI=10.1016/0378-1119(85)90306-3;
RA Legerton T.L., Yanofsky C.;
RT "Cloning and characterization of the multifunctional his-3 gene of
RT Neurospora crassa.";
RL Gene 39:129-140(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-44; VAL-50; PRO-410;
RP ASN-708 AND MET-726.
RC STRAIN=74-OR23-1VA / FGSC 2489, and FGSC 541;
RA Yeadon P.J., Petersen A., Catcheside D.E.A.;
RT "DNA sequence of histidine-3 from two Neurospora wild-types.";
RL Fungal Genet. Newsl. 45:43-43(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33588.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M27531; AAA33588.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF045455; AAC02221.1; -; Genomic_DNA.
DR EMBL; AF045456; AAC02222.1; -; Genomic_DNA.
DR EMBL; BX842637; CAE76555.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA34952.1; -; Genomic_DNA.
DR PIR; A23978; SHNC.
DR RefSeq; XP_964188.1; XM_959095.3.
DR AlphaFoldDB; P07685; -.
DR SMR; P07685; -.
DR STRING; 5141.EFNCRP00000002825; -.
DR EnsemblFungi; EAA34952; EAA34952; NCU03139.
DR GeneID; 3880337; -.
DR KEGG; ncr:NCU03139; -.
DR VEuPathDB; FungiDB:NCU03139; -.
DR HOGENOM; CLU_006732_0_0_1; -.
DR InParanoid; P07685; -.
DR OMA; WEAADLF; -.
DR SABIO-RK; P07685; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd06572; Histidinol_dh; 1.
DR Gene3D; 3.10.20.810; -; 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 PANTHER; PTHR21256; PTHR21256; 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; SSF141734; SSF141734; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Histidine biosynthesis; Hydrolase;
KW Metal-binding; Multifunctional enzyme; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..870
FT /note="Histidine biosynthesis trifunctional protein"
FT /id="PRO_0000135911"
FT REGION 1..285
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 286..367
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT REGION 368..870
FT /note="Histidinol dehydrogenase"
FT ACT_SITE 762
FT /evidence="ECO:0000250"
FT ACT_SITE 763
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 796
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 855
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VARIANT 44
FT /note="Q -> K (in strain: FGSC 541)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 50
FT /note="L -> V (in strain: FGSC 541)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 410
FT /note="L -> P (in strain: FGSC 541)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 708
FT /note="D -> N (in strain: FGSC 541)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 726
FT /note="T -> M (in strain: FGSC 541)"
FT /evidence="ECO:0000269|Ref.2"
FT CONFLICT 604
FT /note="Y -> H (in Ref. 2; AAC02221/AAC02222)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="A -> G (in Ref. 2; AAC02221/AAC02222)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="L -> F (in Ref. 2; AAC02221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 93836 MW; ACE28C977682E120 CRC64;
METTLPLPFL VGVSVPPGLN DIKEGLSREE VSCLGCVFFE VKPQTLEKIL RFLKRHNVEF
EPYFDVTALE SIDDIITLLD AGARKVFVKT EQLADLSAYG SRVAPIVTGS SAALLSSATE
SGLLLSGFDQ TASEAAQFLE EARDKKITPF FIKPVPGADL EQFIQVAAKA NAIPILPSTG
LTTKKDEAGK LAISTILSSV WKSDRPDGLL PTVVVDEHDT ALGLVYSSAE SVNEALRTQT
GVYQSRKRGL WYKGATSGDT QELVRISLDC DNDALKFVVK QKGRFCHLDQ SGCFGQLKGL
PKLEQTLISR KQSAPEGSYT ARLFSDEKLV RAKIMEEAEE LCTAQTPQEI AFEAADLFYF
ALTRAVAAGV TLADIERSLD AKSWKVKRRT GDAKGKWAEK EGIKPAASAL AATSAPVTKE
AAQETTPEKI TMRRFDASKV STEELDAALK RPAQKSSDAI YKIIVPIIED VRKNGDKAVL
SYTHKFEKAT SLTSPVLKAP FPKELMQLPE ETIAAIDVSF ENIRKFHAAQ KEEKPLQVET
MPGVVCSRFS RPIEAVGCYI PGGTAVLPST ALMLGVPAMV AGCNKIVFAS PPRADGTITP
EIVYVAHKVG AESIVLAGGA QAVAAMAYGT ESITKVDKIL GPGNQFVTAA KMFVSNDTNA
AVGIDMPAGP SEVLVIADKD ANPAFVASDL LSQAEHGVDS QVILIAIDLD EEHLQAIEDE
VHRQATELPR VQIVRGSIAH SITVQVKTVE EAMELSNKYA PEHLILQIKE AEKAVDLVMN
AGSVFIGAWT PESVGDYSAG VNHSLPTYGF AKQYSGVNLA SFVKHITSSN LTAEGLKNVG
QAVMQLAKVE ELEAHRRAVS IRLEHMSKSN
