UniProtKB - P62623 (ISPH_ECOLI)

BLAST

>sp|P62623|ISPH_ECOLI 4-hydroxy-3-methylbut-2-enyl diphosphate reductase OS=Escherichia coli (strain K12) OX=83333 GN=ispH PE=1 SV=1
MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQI
SEVPDGAILIFSAHGVSQAVRNEAKSRDLTVFDATCPLVTKVHMEVARASRRGEESILIG
HAGHPEVEGTMGQYSNPEGGMYLVESPDDVWKLTVKNEEKLSFMTQTTLSVDDTSDVIDA
LRKRFPKIVGPRKDDICYATTNRQEAVRALAEQAEVVLVVGSKNSSNSNRLAELAQRMGK
RAFLIDDAKDIQEEWVKEVKCVGVTAGASAPDILVQNVVARLQQLGGGEAIPLEGREENI
VFEVPKELRVDIREVD

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History
Entry version 121 (07 Nov 2018)
Sequence version 1 (19 Jul 2004)
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Protein

4-hydroxy-3-methylbut-2-enyl diphosphate reductase

Gene

ispH

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis (PubMed:11818558, PubMed:11418107, PubMed:12706830, PubMed:19569147, PubMed:22137895). In vitro, can also hydrate acetylenes to aldehydes and ketones via anti-Markovnikov/Markovnikov addition (PubMed:22948824).6 Publications

Catalytic activityⁱ

Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H₂O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H⁺.3 Publications

Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H₂O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H⁺.3 Publications

Cofactorⁱ

[4Fe-4S] cluster5 PublicationsNote: Was shown to bind 1 [3Fe-4S] cluster per subunit (PubMed:19569147, PubMed:20080550, PubMed:15469281). However, it initially contains a [4Fe-4S] cluster which easily degrades into a [3Fe-4S] form in the presence of oxygen (PubMed:12706830, PubMed:22137895, PubMed:20080550, PubMed:22687151).6 Publications

Activity regulationⁱ

Addition of Ca²⁺, Mg²⁺, Mn²⁺, Ni²⁺, Co²⁺ or Fe²⁺ decreases the catalytic activity (PubMed:15469281). Addition of Zn²⁺ results in complete loss of activity (PubMed:15469281). Is potently inhibited by substrate analogs in which the hydroxy group in HMBPP is replaced by an amino or thiol group (PubMed:22012762).2 Publications

Kineticsⁱ

pH dependenceⁱ

Optimum pH is 7.0.

Pathwayⁱ: dimethylallyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate.1 Publication1 Publication
Proteins known to be involved in this subpathway in this organism are:

4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)

This subpathway is part of the pathway dimethylallyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate, the pathway dimethylallyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Pathwayⁱ: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 6 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.1 Publication1 Publication
Proteins known to be involved in the 6 steps of the subpathway in this organism are:

1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD)
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF)
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)

This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	12	Iron-sulfur (4Fe-4S)Combined sources5 Publications	1
Binding siteⁱ	41	SubstrateCombined sources1 Publication2 Publications	1
Binding siteⁱ	74	SubstrateCombined sources1 Publication2 Publications	1
Metal bindingⁱ	96	Iron-sulfur (4Fe-4S)Combined sources5 Publications	1
Binding siteⁱ	124	SubstrateCombined sources1 Publication2 Publications	1
Active siteⁱ	126	Proton donor2 Publications	1
Binding siteⁱ	167	SubstrateCombined sources1 Publication2 Publications	1
Metal bindingⁱ	197	Iron-sulfur (4Fe-4S)Combined sources5 Publications	1
Binding siteⁱ	269	SubstrateCombined sources1 Publication2 Publications	1

GO - Molecular functionⁱ

3 iron, 4 sulfur cluster binding
Source: EcoCyc
Inferred from direct assayⁱ
- 19569147
4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity Source: UniProtKB-UniRule
4 iron, 4 sulfur cluster binding Source: UniProtKB-UniRule
hydroxymethylbutenyl pyrophosphate reductase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 12571359
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

dimethylallyl diphosphate biosynthetic process Source: UniProtKB-UniRule
isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 11418107
terpenoid biosynthetic process Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Isoprene biosynthesis
Ligand	4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11081-MONOMER MetaCyc:EG11081-MONOMER
UniPathwayⁱ	UPA00056;UER00097 UPA00059;UER00105

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase1 Publication (EC:1.17.7.43 Publications) Short name: HMBPP reductase1 Publication Alternative name(s): 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase1 Publication
Gene namesⁱ	Name:ispH1 Publication Synonyms:lytB, yaaE Ordered Locus Names:b0029, JW0027
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11081 ispH

EcoGeneⁱ

EG11081 ispH

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Cells lacking this gene are viable only if the medium is supplemented with mevalonate or the cells are complemented with an episomal copy of ispH (PubMed:11418107). A conditional E.coli lytB mutant shows that LytB is essential for survival and that depletion of LytB results in cell lysis (PubMed:11717301).2 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	12	C → S: Loss of catalytic activity. 2 Publications	1
Mutagenesisⁱ	41	H → N: No effect on catalytic activity. 1 Publication	1
Mutagenesisⁱ	74	H → N: Reduces catalytic activity 2-fold. 1 Publication	1
Mutagenesisⁱ	96	C → S: Loss of catalytic activity. 2 Publications	1
Mutagenesisⁱ	99	V → A: No effect on catalytic activity. 1 Publication	1
Mutagenesisⁱ	124	H → N: Loss of catalytic activity. 1 Publication	1
Mutagenesisⁱ	126	E → D or Q: Loss of catalytic activity. 2 Publications	1
Mutagenesisⁱ	167	T → C: Reduces catalytic activity 3-fold. 2 Publications	1
Mutagenesisⁱ	167	T → S: No effect on catalytic activity. 2 Publications	1
Mutagenesisⁱ	197	C → S: Loss of catalytic activity. 2 Publications	1
Mutagenesisⁱ	225	S → C: Loss of catalytic activity. 1 Publication	1
Mutagenesisⁱ	227	N → Q: Reduces catalytic activity 20-fold. 1 Publication	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB01785 Dimethylallyl Diphosphate DB04714 ISOPENTENYL PYROPHOSPHATE

DrugBankⁱ

DB01785 Dimethylallyl Diphosphate
DB04714 ISOPENTENYL PYROPHOSPHATE

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000128812	1 – 316	4-hydroxy-3-methylbut-2-enyl diphosphate reductaseAdd BLAST		316

Proteomic databases

EPDⁱ	P62623
PaxDbⁱ	P62623
PRIDEⁱ	P62623

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Protein-protein interaction databases

BioGridⁱ	4262917, 331 interactors
Database of interacting proteins More...DIPⁱ	DIP-35808N
IntActⁱ	P62623, 7 interactors
STRINGⁱ	316385.ECDH10B_0030

Chemistry databases

BindingDBⁱ

P62623

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 5	Combined sources	4
Helixⁱ	13 – 29	Combined sources	17
Beta strandⁱ	33 – 37	Combined sources	5
Beta strandⁱ	39 – 41	Combined sources	3
Helixⁱ	43 – 51	Combined sources	9
Beta strandⁱ	54 – 59	Combined sources	6
Helixⁱ	60 – 62	Combined sources	3
Beta strandⁱ	68 – 71	Combined sources	4
Helixⁱ	78 – 86	Combined sources	9
Beta strandⁱ	90 – 93	Combined sources	4
Helixⁱ	97 – 112	Combined sources	16
Beta strandⁱ	115 – 120	Combined sources	6
Helixⁱ	125 – 131	Combined sources	7
Beta strandⁱ	137 – 139	Combined sources	3
Beta strandⁱ	141 – 144	Combined sources	4
Helixⁱ	147 – 152	Combined sources	6
Beta strandⁱ	160 – 165	Combined sources	6
Beta strandⁱ	167 – 169	Combined sources	3
Helixⁱ	171 – 184	Combined sources	14
Beta strandⁱ	191 – 193	Combined sources	3
Helixⁱ	198 – 213	Combined sources	16
Beta strandⁱ	215 – 220	Combined sources	6
Helixⁱ	226 – 237	Combined sources	12
Beta strandⁱ	241 – 247	Combined sources	7
Helixⁱ	248 – 250	Combined sources	3
Helixⁱ	253 – 255	Combined sources	3
Turnⁱ	256 – 258	Combined sources	3
Beta strandⁱ	260 – 266	Combined sources	7
Helixⁱ	272 – 284	Combined sources	13
Beta strandⁱ	289 – 292	Combined sources	4
Beta strandⁱ	300 – 302	Combined sources	3
Helixⁱ	306 – 308	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P62623
SMRⁱ	P62623
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P62623

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	225 – 227	Substrate bindingCombined sources1 Publication2 Publications		3

Sequence similaritiesⁱ

Belongs to the IspH family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105C48 Bacteria COG0761 LUCA
HOGENOMⁱ	HOG000220192
InParanoidⁱ	P62623
KEGG Orthology (KO) More...KOⁱ	K03527
PhylomeDBⁱ	P62623

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd13944 lytB_ispH, 1 hit
HAMAPⁱ	MF_00191 IspH, 1 hit
InterProⁱ	View protein in InterPro IPR003451 LytB/IspH
PANTHERⁱ	PTHR30426 PTHR30426, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02401 LYTB, 1 hit
TIGRFAMsⁱ	TIGR00216 ispH_lytB, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P62623-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MQILLANPRG FCAGVDRAIS IVENALAIYG APIYVRHEVV HNRYVVDSLR 
        60         70         80         90        100
ERGAIFIEQI SEVPDGAILI FSAHGVSQAV RNEAKSRDLT VFDATCPLVT 
       110        120        130        140        150
KVHMEVARAS RRGEESILIG HAGHPEVEGT MGQYSNPEGG MYLVESPDDV 
       160        170        180        190        200
WKLTVKNEEK LSFMTQTTLS VDDTSDVIDA LRKRFPKIVG PRKDDICYAT 
       210        220        230        240        250
TNRQEAVRAL AEQAEVVLVV GSKNSSNSNR LAELAQRMGK RAFLIDDAKD 
       260        270        280        290        300
IQEEWVKEVK CVGVTAGASA PDILVQNVVA RLQQLGGGEA IPLEGREENI 
       310 
VFEVPKELRV DIREVD

Length:316

Mass (Da):34,775

Last modified:July 19, 2004 - v1

Checksum:ⁱ0E7B378BD49AB771

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY062212 Genomic DNA Translation: AAL38655.1 X54945 Genomic DNA Translation: CAA38707.1 U00096 Genomic DNA Translation: AAC73140.1 AP009048 Genomic DNA Translation: BAB96598.1
PIRⁱ	JE0403
NCBI Reference Sequences More...RefSeqⁱ	NP_414570.1, NC_000913.3 WP_001166395.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73140; AAC73140; b0029 BAB96598; BAB96598; BAB96598
GeneIDⁱ	944777
KEGGⁱ	ecj:JW0027 eco:b0029
PATRICⁱ	fig\|1411691.4.peg.2256

Protein	Similar proteins		Species	Score	Length	Source
P62623	4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO24		316	UniRef100_A7ZHB8
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO55		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO57		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO5E		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO7I		316
+133

Protein	Similar proteins		Species	Score	Length	Source
P62623	4-hydroxy-3-methylbut-2-enyl diphosphate reductase		SALTI		316	UniRef90_P58678
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO24		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO55		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO57		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		ECO5E		316
+975

Protein	Similar proteins		Species	Score	Length	Source
P62623	4-hydroxy-3-methylbut-2-enyl diphosphate reductase		SALTI		316	UniRef50_P58678
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		SALPC		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		SHIF8		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		SHIFL		316
4-hydroxy-3-methylbut-2-enyl diphosphate reductase		SALAR		316
+1879

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY062212 Genomic DNA Translation: AAL38655.1 X54945 Genomic DNA Translation: CAA38707.1 U00096 Genomic DNA Translation: AAC73140.1 AP009048 Genomic DNA Translation: BAB96598.1
PIRⁱ	JE0403
RefSeqⁱ	NP_414570.1, NC_000913.3 WP_001166395.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3F7T	X-ray	1.80	A/B	1-316	[»]
	3KE8	X-ray	1.70	A/B	1-316	[»]
	3KE9	X-ray	1.90	A/B	1-316	[»]
	3KEF	X-ray	1.70	A/B	1-316	[»]
	3KEL	X-ray	1.80	A/B	1-316	[»]
	3KEM	X-ray	2.00	A/B	1-316	[»]
	3SZL	X-ray	1.60	A/B	1-316	[»]
	3SZO	X-ray	1.60	A/B	1-316	[»]
	3SZU	X-ray	1.40	A/B	1-316	[»]
	3T0F	X-ray	1.90	A/B	1-316	[»]
	3T0G	X-ray	2.10	A/B	1-316	[»]
	3URK	X-ray	1.50	A/B	1-316	[»]
	3UTC	X-ray	1.90	A/B	1-316	[»]
	3UTD	X-ray	1.70	A/B	1-316	[»]
	3UV3	X-ray	1.60	A/B	1-316	[»]
	3UV6	X-ray	1.70	A/B	1-316	[»]
	3UV7	X-ray	1.60	A/B	1-316	[»]
	3UWM	X-ray	1.80	A/B	1-316	[»]
	3ZGL	X-ray	1.68	A/B	1-316	[»]
	3ZGN	X-ray	1.95	A/B	1-316	[»]
	4EB3	X-ray	1.90	A/B	1-315	[»]
	4H4C	X-ray	1.80	A/B	1-315	[»]
	4H4D	X-ray	1.35	A/B	1-315	[»]
	4H4E	X-ray	1.70	A/B	1-315	[»]
ProteinModelPortalⁱ	P62623
SMRⁱ	P62623
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262917, 331 interactors
DIPⁱ	DIP-35808N
IntActⁱ	P62623, 7 interactors
STRINGⁱ	316385.ECDH10B_0030

Chemistry databases

BindingDBⁱ	P62623
DrugBankⁱ	DB01785 Dimethylallyl Diphosphate DB04714 ISOPENTENYL PYROPHOSPHATE

Proteomic databases

EPDⁱ	P62623
PaxDbⁱ	P62623
PRIDEⁱ	P62623

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73140; AAC73140; b0029 BAB96598; BAB96598; BAB96598
GeneIDⁱ	944777
KEGGⁱ	ecj:JW0027 eco:b0029
PATRICⁱ	fig\|1411691.4.peg.2256

Organism-specific databases

EchoBASEⁱ	EB1073
EcoGeneⁱ	EG11081 ispH

Phylogenomic databases

eggNOGⁱ	ENOG4105C48 Bacteria COG0761 LUCA
HOGENOMⁱ	HOG000220192
InParanoidⁱ	P62623
KOⁱ	K03527
PhylomeDBⁱ	P62623

Enzyme and pathway databases

UniPathwayⁱ	UPA00056;UER00097 UPA00059;UER00105
BioCycⁱ	EcoCyc:EG11081-MONOMER MetaCyc:EG11081-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P62623
Protein Ontology More...PROⁱ	PR:P62623

Family and domain databases

CDDⁱ	cd13944 lytB_ispH, 1 hit
HAMAPⁱ	MF_00191 IspH, 1 hit
InterProⁱ	View protein in InterPro IPR003451 LytB/IspH
PANTHERⁱ	PTHR30426 PTHR30426, 1 hit
Pfamⁱ	View protein in Pfam PF02401 LYTB, 1 hit
TIGRFAMsⁱ	TIGR00216 ispH_lytB, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ISPH_ECOLI
Accessionⁱ	P62623Primary (citable) accession number: P62623 Secondary accession number(s): P22565
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
	Last sequence update:	July 19, 2004
	Last modified:	November 7, 2018
	This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P62623 (ISPH_ECOLI)

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4-hydroxy-3-methylbut-2-enyl diphosphate reductase

ispH

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: dimethylallyl diphosphate biosynthesis

Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: dimethylallyl diphosphate biosynthesis

Pathwayⁱ: isopentenyl diphosphate biosynthesis via DXP pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ