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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: Annotation score: 5 out of 5-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. no protein annotated in this organism
  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

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

SABIO-RKP07685.
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.

PTM / Processingi

Molecule processing

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

Structurei

3D structure databases

ProteinModelPortaliP07685.
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.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. 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.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFiPIRSF001257. His_trifunctional. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP07685.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA34952; EAA34952; NCU03139.
GeneIDi3880337.
KEGGincr:NCU03139.

Organism-specific databases

EuPathDBiFungiDB:NCU03139.

Phylogenomic databases

HOGENOMiHOG000243914.
InParanoidiP07685.
KOiK14152.
OMAiFIGEWTP.
OrthoDBiEOG092C2FQP.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.
SABIO-RKP07685.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. 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.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFiPIRSF001257. His_trifunctional. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS2_NEUCR
AccessioniPrimary (citable) accession number: P07685
Secondary accession number(s): O42788, O42789, Q7RVK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.