Reviewed, UniProtKB/Swiss-Prot P07685 (HIS2_NEUCR)

Names and origin

Protein names

Recommended name:
    Histidine biosynthesis trifunctional protein
Including the following 3 domains:
    1- Recommended name:
            Phosphoribosyl-AMP cyclohydrolase
              EC=3.5.4.19
    2- Recommended name:
            Phosphoribosyl-ATP pyrophosphohydrolase
              EC=3.6.1.31
    3- Recommended name:
            Histidinol dehydrogenase
                Short name=HDH
              EC=1.1.1.23

Gene names

Name:	his-3
ORF Names:	5C2.120, NCU03139

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	870 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. 1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. L-histidinol + 2 NAD+ = L-histidine + 2 NADH.
Cofactor	Binds 1 zinc ion By similarity.
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	ATP-binding Metal-binding NAD Nucleotide-binding Zinc
Molecular function	Hydrolase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NAD or NADH binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: EC phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: EC phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 870	870	Histidine biosynthesis trifunctional protein		PRO_0000135911
Regions
	Region	1 – 285	285	Phosphoribosyl-AMP cyclohydrolase
	Region	286 – 367	82	Phosphoribosyl-ATP pyrophosphohydrolase
	Region	368 – 870	503	Histidinol dehydrogenase
Sites
	Active site	762	1	By similarity
	Active site	763	1	By similarity
	Metal binding	693	1	Zinc By similarity
	Metal binding	696	1	Zinc By similarity
	Metal binding	796	1	Zinc By similarity
	Metal binding	855	1	Zinc By similarity
Natural variations
	Natural variant	44	1	Q → K in strain: FGSC 541. Ref.2
	Natural variant	50	1	L → V in strain: FGSC 541. Ref.2
	Natural variant	410	1	L → P in strain: FGSC 541. Ref.2
	Natural variant	708	1	D → N in strain: FGSC 541. Ref.2
	Natural variant	726	1	T → M in strain: FGSC 541. Ref.2
Experimental info
	Sequence conflict	604	1	Y → H in AAC02221. Ref.2
	Sequence conflict	604	1	Y → H in AAC02222. Ref.2
	Sequence conflict	811	1	A → G in AAC02221. Ref.2
	Sequence conflict	811	1	A → G in AAC02222. Ref.2
	Sequence conflict	819	1	L → F in AAC02221. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P07685-1 [UniParc]. Last modified June 7, 2005. Version 3. Checksum: ACE28C977682E120	FASTA	870	93,836
	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

References

	« Hide 'large scale' referencesShow '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: 3005109] [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: 12655011] [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. , 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: 12712197] [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
EMBLGenBankDDBJ	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. AABX02000009 Genomic DNA. Translation: EAA34952.1.
PIR	SHNC. A23978.
RefSeq	XP_964188.1.
3D structure databases
HSSP	HSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBase	Search...
Genome annotation databases
GeneID	3880337.
KEGG	ncr:NCU03139.
NMPDR	fig|5141.1.peg.8508.
Enzyme and pathway databases
BRENDA	1.1.1.23. 266. 3.5.4.19. 266. 3.6.1.31. 266.
Family and domain databases
InterPro	IPR016298. Histidine_synth_trifunct. IPR001692. Histidinol_DH_CS. IPR012131. Hstdl_DH_prok-type. IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. [Graphical view]
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
PIRSF	PIRSF001257. His_trifunctional. 1 hit.
PRINTS	PR00083. HOLDHDRGNASE.
ProDom	PD002680. Histidinol_dh. 1 hit. PD002610. PRA_cyclohydro. 1 hit. PD002611. Pra_PH/CH. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00069. hisD. 1 hit. TIGR03188. histidine_hisI. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS2_NEUCR

Accession

Primary (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:	June 16, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)