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Protein

Histidine biosynthesis trifunctional protein

Gene

his-3

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.
1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.
L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Pathwayi: L-histidine biosynthesis

This protein is involved in step 2, 3 and 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Histidine biosynthesis trifunctional protein (his-3)
  3. Histidine biosynthesis trifunctional protein (his-3)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (his-7)
  5. Imidazole glycerol phosphate synthase hisHF (his-6)
  6. Imidazoleglycerol-phosphate dehydratase (65E11.030)
  7. no protein annotated in this organism
  8. no protein annotated in this organism
  9. Histidine biosynthesis trifunctional protein (his-3)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi693ZincBy similarity1
Metal bindingi696ZincBy similarity1
Active sitei762By similarity1
Active sitei763By similarity1
Metal bindingi796ZincBy similarity1
Metal bindingi855ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Oxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandATP-binding, Metal-binding, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

SABIO-RKiP07685
UniPathwayiUPA00031; UER00007
UPA00031; UER00008
UPA00031; UER00014

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine biosynthesis trifunctional protein
Including the following 3 domains:
Phosphoribosyl-AMP cyclohydrolase (EC:3.5.4.19)
Phosphoribosyl-ATP pyrophosphohydrolase (EC:3.6.1.31)
Histidinol dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:his-3
ORF Names:5C2.120, NCU03139
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 1, Linkage Group I

Organism-specific databases

EuPathDBiFungiDB:NCU03139

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001359111 – 870Histidine biosynthesis trifunctional proteinAdd BLAST870

Proteomic databases

PRIDEiP07685

Structurei

3D structure databases

ProteinModelPortaliP07685
SMRiP07685
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 285Phosphoribosyl-AMP cyclohydrolaseAdd BLAST285
Regioni286 – 367Phosphoribosyl-ATP pyrophosphohydrolaseAdd BLAST82
Regioni368 – 870Histidinol dehydrogenaseAdd BLAST503

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000243914
InParanoidiP07685
KOiK14152
OMAiFIGEWTP
OrthoDBiEOG092C2FQP

Family and domain databases

CDDicd06572 Histidinol_dh, 1 hit
Gene3Di3.10.20.400, 1 hit
HAMAPiMF_01024 HisD, 1 hit
InterProiView protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR008179 HisE
IPR016298 Histidine_synth_trifunct
IPR001692 Histidinol_DH_CS
IPR012131 Hstdl_DH
IPR021130 PRib-ATP_PPHydrolase-like
IPR002496 PRib_AMP_CycHydrolase_dom
IPR038019 PRib_AMP_CycHydrolase_sf
PANTHERiPTHR21256 PTHR21256, 1 hit
PfamiView protein in Pfam
PF00815 Histidinol_dh, 1 hit
PF01502 PRA-CH, 1 hit
PF01503 PRA-PH, 1 hit
PIRSFiPIRSF001257 His_trifunctional, 1 hit
PRINTSiPR00083 HOLDHDRGNASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002610 PRA_CycHdrlase, 1 hit
SUPFAMiSSF141734 SSF141734, 1 hit
SSF53720 SSF53720, 1 hit
TIGRFAMsiTIGR00069 hisD, 1 hit
TIGR03188 histidine_hisI, 1 hit
PROSITEiView protein in PROSITE
PS00611 HISOL_DEHYDROGENASE, 1 hit

Sequencei

Sequence statusi: Complete.

P07685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METTLPLPFL VGVSVPPGLN DIKEGLSREE VSCLGCVFFE VKPQTLEKIL
60 70 80 90 100
RFLKRHNVEF EPYFDVTALE SIDDIITLLD AGARKVFVKT EQLADLSAYG
110 120 130 140 150
SRVAPIVTGS SAALLSSATE SGLLLSGFDQ TASEAAQFLE EARDKKITPF
160 170 180 190 200
FIKPVPGADL EQFIQVAAKA NAIPILPSTG LTTKKDEAGK LAISTILSSV
210 220 230 240 250
WKSDRPDGLL PTVVVDEHDT ALGLVYSSAE SVNEALRTQT GVYQSRKRGL
260 270 280 290 300
WYKGATSGDT QELVRISLDC DNDALKFVVK QKGRFCHLDQ SGCFGQLKGL
310 320 330 340 350
PKLEQTLISR KQSAPEGSYT ARLFSDEKLV RAKIMEEAEE LCTAQTPQEI
360 370 380 390 400
AFEAADLFYF ALTRAVAAGV TLADIERSLD AKSWKVKRRT GDAKGKWAEK
410 420 430 440 450
EGIKPAASAL AATSAPVTKE AAQETTPEKI TMRRFDASKV STEELDAALK
460 470 480 490 500
RPAQKSSDAI YKIIVPIIED VRKNGDKAVL SYTHKFEKAT SLTSPVLKAP
510 520 530 540 550
FPKELMQLPE ETIAAIDVSF ENIRKFHAAQ KEEKPLQVET MPGVVCSRFS
560 570 580 590 600
RPIEAVGCYI PGGTAVLPST ALMLGVPAMV AGCNKIVFAS PPRADGTITP
610 620 630 640 650
EIVYVAHKVG AESIVLAGGA QAVAAMAYGT ESITKVDKIL GPGNQFVTAA
660 670 680 690 700
KMFVSNDTNA AVGIDMPAGP SEVLVIADKD ANPAFVASDL LSQAEHGVDS
710 720 730 740 750
QVILIAIDLD EEHLQAIEDE VHRQATELPR VQIVRGSIAH SITVQVKTVE
760 770 780 790 800
EAMELSNKYA PEHLILQIKE AEKAVDLVMN AGSVFIGAWT PESVGDYSAG
810 820 830 840 850
VNHSLPTYGF AKQYSGVNLA SFVKHITSSN LTAEGLKNVG QAVMQLAKVE
860 870
ELEAHRRAVS IRLEHMSKSN
Length:870
Mass (Da):93,836
Last modified:June 7, 2005 - v3
Checksum:iACE28C977682E120
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti604Y → H in AAC02221 (Ref. 2) Curated1
Sequence conflicti604Y → H in AAC02222 (Ref. 2) Curated1
Sequence conflicti811A → G in AAC02221 (Ref. 2) Curated1
Sequence conflicti811A → G in AAC02222 (Ref. 2) Curated1
Sequence conflicti819L → F in AAC02221 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti44Q → K in strain: FGSC 541. 1 Publication1
Natural varianti50L → V in strain: FGSC 541. 1 Publication1
Natural varianti410L → P in strain: FGSC 541. 1 Publication1
Natural varianti708D → N in strain: FGSC 541. 1 Publication1
Natural varianti726T → M in strain: FGSC 541. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA23978 SHNC
RefSeqiXP_964188.1, XM_959095.3

Genome annotation databases

EnsemblFungiiEAA34952; EAA34952; NCU03139
GeneIDi3880337
KEGGincr:NCU03139

Similar proteinsi

Entry informationi

Entry nameiHIS2_NEUCR
AccessioniPrimary (citable) accession number: P07685
Secondary accession number(s): O42788, O42789, Q7RVK0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: May 23, 2018
This is version 145 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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