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Histidine biosynthesis trifunctional protein [Includes: Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19); Phosphoribosyl-ATP pyrophosphohydrolase (EC 3.6.1.31); Histidinol dehydrogenase (HDH) (EC 1.1.1.23)]

 HIS2_NEUCR              Reviewed;         870 AA.
P07685; O42788; O42789; Q7RVK0;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 3.
23-MAY-2018, entry version 145.
RecName: Full=Histidine biosynthesis trifunctional protein;
Includes:
RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
EC=3.5.4.19;
Includes:
RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase;
EC=3.6.1.31;
Includes:
RecName: Full=Histidinol dehydrogenase;
Short=HDH;
EC=1.1.1.23;
Name=his-3; ORFNames=5C2.120, NCU03139;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=74-OR23-1VA / FGSC 2489;
PubMed=3005109; DOI=10.1016/0378-1119(85)90306-3;
Legerton T.L., Yanofsky C.;
"Cloning and characterization of the multifunctional his-3 gene of
Neurospora crassa.";
Gene 39:129-140(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-44; VAL-50;
PRO-410; ASN-708 AND MET-726.
STRAIN=74-OR23-1VA / FGSC 2489, and FGSC 541;
Yeadon P.J., Petersen A., Catcheside D.E.A.;
"DNA sequence of histidine-3 from two Neurospora wild-types.";
Fungal Genet. Newsl. 45:43-43(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
-!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1-
(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-
ribosylamino)methylideneamino)imidazole-4-carboxamide.
-!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1-
(5-phospho-beta-D-ribosyl)-AMP + diphosphate.
-!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine
+ 2 NADH.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion. {ECO:0000250};
-!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
-!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
-!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
-!- SIMILARITY: In the C-terminal section; belongs to the histidinol
dehydrogenase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA33588.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; M27531; AAA33588.1; ALT_FRAME; Genomic_DNA.
EMBL; AF045455; AAC02221.1; -; Genomic_DNA.
EMBL; AF045456; AAC02222.1; -; Genomic_DNA.
EMBL; BX842637; CAE76555.1; -; Genomic_DNA.
EMBL; CM002236; EAA34952.1; -; Genomic_DNA.
PIR; A23978; SHNC.
RefSeq; XP_964188.1; XM_959095.3.
ProteinModelPortal; P07685; -.
SMR; P07685; -.
PRIDE; P07685; -.
EnsemblFungi; EAA34952; EAA34952; NCU03139.
GeneID; 3880337; -.
KEGG; ncr:NCU03139; -.
EuPathDB; FungiDB:NCU03139; -.
HOGENOM; HOG000243914; -.
InParanoid; P07685; -.
KO; K14152; -.
OMA; FIGEWTP; -.
OrthoDB; EOG092C2FQP; -.
SABIO-RK; P07685; -.
UniPathway; UPA00031; UER00007.
UniPathway; UPA00031; UER00008.
UniPathway; UPA00031; UER00014.
Proteomes; UP000001805; Chromosome 1, Linkage Group I.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004399; F:histidinol dehydrogenase activity; IBA:GO_Central.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
CDD; cd06572; Histidinol_dh; 1.
Gene3D; 3.10.20.400; -; 1.
HAMAP; MF_01024; HisD; 1.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR008179; HisE.
InterPro; IPR016298; Histidine_synth_trifunct.
InterPro; IPR001692; Histidinol_DH_CS.
InterPro; IPR012131; Hstdl_DH.
InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
PANTHER; PTHR21256; PTHR21256; 1.
Pfam; PF00815; Histidinol_dh; 1.
Pfam; PF01502; PRA-CH; 1.
Pfam; PF01503; PRA-PH; 1.
PIRSF; PIRSF001257; His_trifunctional; 1.
PRINTS; PR00083; HOLDHDRGNASE.
ProDom; PD002610; PRA_CycHdrlase; 1.
SUPFAM; SSF141734; SSF141734; 1.
SUPFAM; SSF53720; SSF53720; 1.
TIGRFAMs; TIGR00069; hisD; 1.
TIGRFAMs; TIGR03188; histidine_hisI; 1.
PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
3: Inferred from homology;
Amino-acid biosynthesis; ATP-binding; Complete proteome;
Histidine biosynthesis; Hydrolase; Metal-binding;
Multifunctional enzyme; NAD; Nucleotide-binding; Oxidoreductase;
Reference proteome; Zinc.
CHAIN 1 870 Histidine biosynthesis trifunctional
protein.
/FTId=PRO_0000135911.
REGION 1 285 Phosphoribosyl-AMP cyclohydrolase.
REGION 286 367 Phosphoribosyl-ATP pyrophosphohydrolase.
REGION 368 870 Histidinol dehydrogenase.
ACT_SITE 762 762 {ECO:0000250}.
ACT_SITE 763 763 {ECO:0000250}.
METAL 693 693 Zinc. {ECO:0000250}.
METAL 696 696 Zinc. {ECO:0000250}.
METAL 796 796 Zinc. {ECO:0000250}.
METAL 855 855 Zinc. {ECO:0000250}.
VARIANT 44 44 Q -> K (in strain: FGSC 541).
{ECO:0000269|Ref.2}.
VARIANT 50 50 L -> V (in strain: FGSC 541).
{ECO:0000269|Ref.2}.
VARIANT 410 410 L -> P (in strain: FGSC 541).
{ECO:0000269|Ref.2}.
VARIANT 708 708 D -> N (in strain: FGSC 541).
{ECO:0000269|Ref.2}.
VARIANT 726 726 T -> M (in strain: FGSC 541).
{ECO:0000269|Ref.2}.
CONFLICT 604 604 Y -> H (in Ref. 2; AAC02221/AAC02222).
{ECO:0000305}.
CONFLICT 811 811 A -> G (in Ref. 2; AAC02221/AAC02222).
{ECO:0000305}.
CONFLICT 819 819 L -> F (in Ref. 2; AAC02221).
{ECO:0000305}.
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


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