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P07685 (HIS2_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine biosynthesis trifunctional protein

Including the following 3 domains:

  1. Phosphoribosyl-AMP cyclohydrolase
    EC=3.5.4.19
  2. Phosphoribosyl-ATP pyrophosphohydrolase
    EC=3.6.1.31
  3. Histidinol dehydrogenase
    Short name=HDH
    EC=1.1.1.23
Gene names
Name:his-3
ORF Names:5C2.120, NCU03139
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length870 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP-Rule MF_01024

1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate. HAMAP-Rule MF_01024

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP-Rule MF_01024

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.

Sequence similarities

In the C-terminal section; belongs to the histidinol dehydrogenase family.

Sequence caution

The sequence AAA33588.1 differs from that shown. Reason: Frameshift at several positions.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 870870Histidine biosynthesis trifunctional protein HAMAP-Rule MF_01024
PRO_0000135911

Regions

Region1 – 285285Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01024
Region286 – 36782Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01024
Region368 – 870503Histidinol dehydrogenase HAMAP-Rule MF_01024

Sites

Active site7621 By similarity
Active site7631 By similarity
Metal binding6931Zinc By similarity
Metal binding6961Zinc By similarity
Metal binding7961Zinc By similarity
Metal binding8551Zinc By similarity

Natural variations

Natural variant441Q → K in strain: FGSC 541. Ref.2
Natural variant501L → V in strain: FGSC 541. Ref.2
Natural variant4101L → P in strain: FGSC 541. Ref.2
Natural variant7081D → N in strain: FGSC 541. Ref.2
Natural variant7261T → M in strain: FGSC 541. Ref.2

Experimental info

Sequence conflict6041Y → H in AAC02221. Ref.2
Sequence conflict6041Y → H in AAC02222. Ref.2
Sequence conflict8111A → G in AAC02221. Ref.2
Sequence conflict8111A → G in AAC02222. Ref.2
Sequence conflict8191L → F in AAC02221. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07685 [UniParc].

Last modified June 7, 2005. Version 3.
Checksum: ACE28C977682E120

FASTA87093,836
        10         20         30         40         50         60 
METTLPLPFL VGVSVPPGLN DIKEGLSREE VSCLGCVFFE VKPQTLEKIL RFLKRHNVEF 

        70         80         90        100        110        120 
EPYFDVTALE SIDDIITLLD AGARKVFVKT EQLADLSAYG SRVAPIVTGS SAALLSSATE 

       130        140        150        160        170        180 
SGLLLSGFDQ TASEAAQFLE EARDKKITPF FIKPVPGADL EQFIQVAAKA NAIPILPSTG 

       190        200        210        220        230        240 
LTTKKDEAGK LAISTILSSV WKSDRPDGLL PTVVVDEHDT ALGLVYSSAE SVNEALRTQT 

       250        260        270        280        290        300 
GVYQSRKRGL WYKGATSGDT QELVRISLDC DNDALKFVVK QKGRFCHLDQ SGCFGQLKGL 

       310        320        330        340        350        360 
PKLEQTLISR KQSAPEGSYT ARLFSDEKLV RAKIMEEAEE LCTAQTPQEI AFEAADLFYF 

       370        380        390        400        410        420 
ALTRAVAAGV TLADIERSLD AKSWKVKRRT GDAKGKWAEK EGIKPAASAL AATSAPVTKE 

       430        440        450        460        470        480 
AAQETTPEKI TMRRFDASKV STEELDAALK RPAQKSSDAI YKIIVPIIED VRKNGDKAVL 

       490        500        510        520        530        540 
SYTHKFEKAT SLTSPVLKAP FPKELMQLPE ETIAAIDVSF ENIRKFHAAQ KEEKPLQVET 

       550        560        570        580        590        600 
MPGVVCSRFS RPIEAVGCYI PGGTAVLPST ALMLGVPAMV AGCNKIVFAS PPRADGTITP 

       610        620        630        640        650        660 
EIVYVAHKVG AESIVLAGGA QAVAAMAYGT ESITKVDKIL GPGNQFVTAA KMFVSNDTNA 

       670        680        690        700        710        720 
AVGIDMPAGP SEVLVIADKD ANPAFVASDL LSQAEHGVDS QVILIAIDLD EEHLQAIEDE 

       730        740        750        760        770        780 
VHRQATELPR VQIVRGSIAH SITVQVKTVE EAMELSNKYA PEHLILQIKE AEKAVDLVMN 

       790        800        810        820        830        840 
AGSVFIGAWT PESVGDYSAG VNHSLPTYGF AKQYSGVNLA SFVKHITSSN LTAEGLKNVG 

       850        860        870 
QAVMQLAKVE ELEAHRRAVS IRLEHMSKSN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the multifunctional his-3 gene of Neurospora crassa."
Legerton T.L., Yanofsky C.
Gene 39:129-140(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 74-OR23-1VA / FGSC 2489.
[2]"DNA sequence of histidine-3 from two Neurospora wild-types."
Yeadon P.J., Petersen A., Catcheside D.E.A.
Fungal Genet. Newsl. 45:43-43(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-44; VAL-50; PRO-410; ASN-708 AND MET-726.
Strain: 74-OR23-1VA / FGSC 2489 and FGSC 541.
[3]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[4]"The genome sequence of the filamentous fungus Neurospora crassa."
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. expand/collapse author list , 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.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27531 Genomic DNA. Translation: AAA33588.1. Frameshift.
AF045455 Genomic DNA. Translation: AAC02221.1.
AF045456 Genomic DNA. Translation: AAC02222.1.
BX842637 Genomic DNA. Translation: CAE76555.1.
CM002236 Genomic DNA. Translation: EAA34952.1.
PIRSHNC. A23978.
RefSeqXP_964188.1. XM_959095.2.
UniGeneNcr.7165.

3D structure databases

ProteinModelPortalP07685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU03139.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000002825; EFNCRP00000002825; EFNCRG00000002822.
GeneID3880337.
KEGGncr:NCU03139.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK14152.
OMANIRKFHA.
OrthoDBEOG7DJSVM.

Enzyme and pathway databases

SABIO-RKP07685.
UniPathwayUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016298. Histidine_synth_trifunct.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
IPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFPIRSF001257. His_trifunctional. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
ProDomPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS2_NEUCR
AccessionPrimary (citable) accession number: P07685
Secondary accession number(s): O42788, O42789, Q7RVK0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: February 19, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways