UniProtKB - P0A6B7 (ISCS_ECOLI)

BLAST

>sp|P0A6B7|ISCS_ECOLI Cysteine desulfurase IscS OS=Escherichia coli (strain K12) OX=83333 GN=iscS PE=1 SV=1
MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIAD
LVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFE
VTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVD
ATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMR
SGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNI
LNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRF
TTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH

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History
Entry version 123 (07 Nov 2018)
Sequence version 1 (07 Jun 2005)
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Protein

Cysteine desulfurase IscS

Gene

iscS

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to an acceptor protein. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Transfers sulfur onto 'Cys-456' of ThiI and onto 'Cys-19' of TusA in transpersulfidation reactions.10 Publications

Catalytic activityⁱ

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.UniRule annotation1 Publication

Cofactorⁱ

pyridoxal 5'-phosphateUniRule annotation2 Publications

Activity regulationⁱ

Treatment with N-ethylmaleimide inhibits sulfur transfer. Activated by ThiI and TusA.3 Publications

Kineticsⁱ

kcat is 8.5 min(-1).1 Publication

K_M=
2.7 µM for L-cysteine
1 Publication
Manual assertion based on experiment inⁱ
- Ref.13
  "Transfer of sulfur from IscS to IscU during Fe/S cluster assembly."
  Urbina H.D., Silberg J.J., Hoff K.G., Vickery L.E.
  J. Biol. Chem. 276:44521-44526(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN SULFUR TRANSFER, INTERACTION WITH ISCU, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF 376-SER--HIS-404.

Pathwayⁱ: iron-sulfur cluster biosynthesis

This protein is involved in the pathway iron-sulfur cluster biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway iron-sulfur cluster biosynthesis and in Cofactor biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	155	Pyridoxal phosphateUniRule annotation	1
Binding siteⁱ	183	Pyridoxal phosphateUniRule annotation1 Publication	1
Binding siteⁱ	243	Pyridoxal phosphateUniRule annotation1 Publication	1
Active siteⁱ	328	Cysteine persulfide intermediateUniRule annotation2 Publications	1
Metal bindingⁱ	328	Iron-sulfur (2Fe-2S); via persulfide group; shared with IscUUniRule annotation	1

GO - Molecular functionⁱ

2 iron, 2 sulfur cluster binding Source: UniProtKB-UniRule
cysteine desulfurase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 10739946
metal ion binding Source: UniProtKB-KW
pyridoxal phosphate binding
Source: EcoCyc
Inferred from direct assayⁱ
- 10600118
selenocysteine lyase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 10739946
sulfur carrier activity
Source: EcoCyc
Inferred from experimentⁱ
- 10739946

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

[2Fe-2S] cluster assembly Source: UniProtKB-UniRule
iron-sulfur cluster assembly
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 10393315
oxazole or thiazole biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 10781607
tRNA pseudouridine synthesis
Source: EcoCyc
Inferred from direct assayⁱ
- 10600118

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	tRNA processing
Ligand	2Fe-2S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7325-MONOMER MetaCyc:G7325-MONOMER
UniPathwayⁱ	UPA00266

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cysteine desulfurase IscS1 PublicationUniRule annotation (EC:2.8.1.7UniRule annotation1 Publication) Alternative name(s): NifS protein homolog1 Publication ThiI transpersulfidase1 Publication TusA transpersulfidase1 Publication
Gene namesⁱ	Name:iscSUniRule annotation Synonyms:nuvC, yfhO, yzzO Ordered Locus Names:b2530, JW2514
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	EG12677 iscS

EcoGeneⁱ

EG12677 iscS

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00331
Curated

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Cells lacking this gene lose sulfurtransferase activity and require thiamine and nicotinic acid for growth. Under aerobic conditions the deletion of IscS causes an auxotrophy for thiamine and nicotinic acid, whereas under anaerobic conditions, only nicotinic acid s required.2 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	328	C → A: Loss of cysteine desulfurization. 1 Publication		1
Mutagenesisⁱ	376 – 404	Missing : Normal cysteine desulfurase activity, decreased binding to IscU, decreased sulfur transfer to IscU, decreased Fe-S cluster assembly. 1 PublicationAdd BLAST		29

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000150264	1 – 404	Cysteine desulfurase IscSAdd BLAST		404

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	206	N6-(pyridoxal phosphate)lysineUniRule annotation1 Publication		1

Proteomic databases

EPDⁱ	P0A6B7
PaxDbⁱ	P0A6B7
PRIDEⁱ	P0A6B7

Interactionⁱ

Subunit structureⁱ

Homodimer. The homodimer interacts with IscU and TusA, other S acceptors. Each subunit of the IscS dimer contacts a IscU monomer.4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
cyaY	P27838	2	EBI-550055,EBI-9146621
fdx	P0A9R4	2	EBI-550055,EBI-767037
iscU	P0ACD4	12	EBI-550055,EBI-561646
rhdA	P52197	2	EBI-550055,EBI-7906952	From Azotobacter vinelandii.
tusA	P0A890	7	EBI-550055,EBI-561780
yfhJ	Q1R8K8	2	EBI-550055,EBI-15582429	From Escherichia coli (strain UTI89 / UPEC).

Protein-protein interaction databases

BioGridⁱ	4263511, 579 interactors 851343, 1 interactor
ComplexPortalⁱ	CPX-2136 L-cysteine desulfurase complex CPX-2139 IscS-TusA complex CPX-2140 IscS-ThiL complex CPX-2141 IscS-IscU complex
Database of interacting proteins More...DIPⁱ	DIP-29109N
IntActⁱ	P0A6B7, 47 interactors
Molecular INTeraction database More...MINTⁱ	P0A6B7
STRINGⁱ	316385.ECDH10B_2697

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 6	Combined sources	3
Turnⁱ	9 – 11	Combined sources	3
Helixⁱ	17 – 23	Combined sources	7
Helixⁱ	24 – 26	Combined sources	3
Helixⁱ	42 – 62	Combined sources	21
Helixⁱ	66 – 68	Combined sources	3
Beta strandⁱ	69 – 73	Combined sources	5
Helixⁱ	75 – 90	Combined sources	16
Helixⁱ	91 – 93	Combined sources	3
Beta strandⁱ	96 – 100	Combined sources	5
Helixⁱ	105 – 116	Combined sources	12
Beta strandⁱ	120 – 124	Combined sources	5
Helixⁱ	134 – 140	Combined sources	7
Beta strandⁱ	145 – 149	Combined sources	5
Turnⁱ	155 – 157	Combined sources	3
Helixⁱ	163 – 173	Combined sources	11
Beta strandⁱ	176 – 180	Combined sources	5
Turnⁱ	182 – 187	Combined sources	6
Turnⁱ	192 – 194	Combined sources	3
Beta strandⁱ	198 – 204	Combined sources	7
Turnⁱ	205 – 208	Combined sources	4
Beta strandⁱ	214 – 218	Combined sources	5
Turnⁱ	220 – 223	Combined sources	4
Turnⁱ	235 – 239	Combined sources	5
Helixⁱ	246 – 279	Combined sources	34
Turnⁱ	280 – 283	Combined sources	4
Beta strandⁱ	287 – 291	Combined sources	5
Turnⁱ	293 – 295	Combined sources	3
Beta strandⁱ	300 – 305	Combined sources	6
Helixⁱ	310 – 316	Combined sources	7
Turnⁱ	317 – 319	Combined sources	3
Helixⁱ	337 – 342	Combined sources	6
Helixⁱ	346 – 350	Combined sources	5
Beta strandⁱ	352 – 356	Combined sources	5
Helixⁱ	363 – 382	Combined sources	20
Helixⁱ	385 – 390	Combined sources	6

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A6B7
SMRⁱ	P0A6B7
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A6B7

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	75 – 76	Pyridoxal phosphate bindingUniRule annotation		2
Regionⁱ	203 – 205	Pyridoxal phosphate bindingUniRule annotation1 Publication		3

Domainⁱ

The C-terminus (residues 376-404) is important for interaction with IscU.1 Publication

Sequence similaritiesⁱ

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105C3J Bacteria COG1104 LUCA
HOGENOMⁱ	HOG000017510
InParanoidⁱ	P0A6B7
KEGG Orthology (KO) More...KOⁱ	K04487
PhylomeDBⁱ	P0A6B7

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
HAMAPⁱ	MF_00331 Cys_desulf_IscS, 1 hit
InterProⁱ	View protein in InterPro IPR000192 Aminotrans_V_dom IPR020578 Aminotrans_V_PyrdxlP_BS IPR010240 Cys_deSase_IscS IPR016454 Cysteine_dSase IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major
PANTHERⁱ	PTHR11601:SF34 PTHR11601:SF34, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00266 Aminotran_5, 1 hit
PIRSFⁱ	PIRSF005572 NifS, 1 hit
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
TIGRFAMsⁱ	TIGR02006 IscS, 1 hit
PROSITEⁱ	View protein in PROSITE PS00595 AA_TRANSFER_CLASS_5, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0A6B7-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKLPIYLDYS ATTPVDPRVA EKMMQFMTMD GTFGNPASRS HRFGWQAEEA 
        60         70         80         90        100
VDIARNQIAD LVGADPREIV FTSGATESDN LAIKGAANFY QKKGKHIITS 
       110        120        130        140        150
KTEHKAVLDT CRQLEREGFE VTYLAPQRNG IIDLKELEAA MRDDTILVSI 
       160        170        180        190        200
MHVNNEIGVV QDIAAIGEMC RARGIIYHVD ATQSVGKLPI DLSQLKVDLM 
       210        220        230        240        250
SFSGHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR SGTLPVHQIV 
       260        270        280        290        300
GMGEAYRIAK EEMATEMERL RGLRNRLWNG IKDIEEVYLN GDLEHGAPNI 
       310        320        330        340        350
LNVSFNYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH 
       360        370        380        390        400
SSIRFSLGRF TTEEEIDYTI ELVRKSIGRL RDLSPLWEMY KQGVDLNSIE 

WAHH

Length:404

Mass (Da):45,090

Last modified:June 7, 2005 - v1

Checksum:ⁱ1E4F2E6F9CD266B0

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	31	G → D AA sequence (PubMed:8663056).Curated	1
Sequence conflictⁱ	34	G → F AA sequence (PubMed:8663056).Curated	1
Sequence conflictⁱ	37 – 38	AS → NA AA sequence (PubMed:8663056).Curated	2
Sequence conflictⁱ	118	G → L AA sequence (PubMed:8663056).Curated	1
Sequence conflictⁱ	126	P → M AA sequence (PubMed:8663056).Curated	1
Sequence conflictⁱ	320	L → I AA sequence (PubMed:8663056).Curated	1
Sequence conflictⁱ	326 – 327	SA → YL AA sequence (PubMed:8663056).Curated	2
Sequence conflictⁱ	339	L → V AA sequence (PubMed:8663056).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAT48142.1 AP009048 Genomic DNA Translation: BAA16424.1
NCBI Reference Sequences More...RefSeqⁱ	WP_001295373.1, NZ_LN832404.1 YP_026169.1, NC_000913.3

Genome annotation databases

EnsemblBacteriaⁱ	AAT48142; AAT48142; b2530 BAA16424; BAA16424; BAA16424
GeneIDⁱ	947004
KEGGⁱ	ecj:JW2514 eco:b2530
PATRICⁱ	fig\|1411691.4.peg.4204

Protein	Similar proteins		Species	Score	Length	Source
P0A6B7	Cysteine desulfurase IscS		ECO24		404	UniRef100_A7ZPX4
Cysteine desulfurase IscS		ECO27		404
Cysteine desulfurase IscS		ECO45		404
Cysteine desulfurase IscS		ECO55		404
Cysteine desulfurase IscS	)	ECO57		404
+215

Protein	Similar proteins		Species	Score	Length	Source
P0A6B7	Cysteine desulfurase IscS		PECCP		404	UniRef90_C6DBJ1
Cysteine desulfurase IscS		CROS8		404
Cysteine desulfurase IscS		ENT38		404
Cysteine desulfurase IscS		ESCF3		404
Cysteine desulfurase IscS		KLEP3		404
+1214

Protein	Similar proteins		Species	Score	Length	Source
P0A6B7	Cysteine desulfurase IscS		PECCP		404	UniRef50_C6DBJ1
Cysteine desulfurase IscS		SALTI		404
Cysteine desulfurase IscS		SALA4		404
Cysteine desulfurase IscS		SALCH		404
Cysteine desulfurase IscS		SALDC		404
+1367

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAT48142.1 AP009048 Genomic DNA Translation: BAA16424.1
RefSeqⁱ	WP_001295373.1, NZ_LN832404.1 YP_026169.1, NC_000913.3

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
	1P3W	X-ray	2.10	A/B	1-404	[»]
ProteinModelPortalⁱ	P0A6B7
SMRⁱ	P0A6B7
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263511, 579 interactors 851343, 1 interactor
ComplexPortalⁱ	CPX-2136 L-cysteine desulfurase complex CPX-2139 IscS-TusA complex CPX-2140 IscS-ThiL complex CPX-2141 IscS-IscU complex
DIPⁱ	DIP-29109N
IntActⁱ	P0A6B7, 47 interactors
MINTⁱ	P0A6B7
STRINGⁱ	316385.ECDH10B_2697

Proteomic databases

EPDⁱ	P0A6B7
PaxDbⁱ	P0A6B7
PRIDEⁱ	P0A6B7

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAT48142; AAT48142; b2530 BAA16424; BAA16424; BAA16424
GeneIDⁱ	947004
KEGGⁱ	ecj:JW2514 eco:b2530
PATRICⁱ	fig\|1411691.4.peg.4204

Organism-specific databases

EchoBASEⁱ	EB2542
EcoGeneⁱ	EG12677 iscS

Phylogenomic databases

eggNOGⁱ	ENOG4105C3J Bacteria COG1104 LUCA
HOGENOMⁱ	HOG000017510
InParanoidⁱ	P0A6B7
KOⁱ	K04487
PhylomeDBⁱ	P0A6B7

Enzyme and pathway databases

UniPathwayⁱ	UPA00266
BioCycⁱ	EcoCyc:G7325-MONOMER MetaCyc:G7325-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0A6B7
Protein Ontology More...PROⁱ	PR:P0A6B7

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
HAMAPⁱ	MF_00331 Cys_desulf_IscS, 1 hit
InterProⁱ	View protein in InterPro IPR000192 Aminotrans_V_dom IPR020578 Aminotrans_V_PyrdxlP_BS IPR010240 Cys_deSase_IscS IPR016454 Cysteine_dSase IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major
PANTHERⁱ	PTHR11601:SF34 PTHR11601:SF34, 1 hit
Pfamⁱ	View protein in Pfam PF00266 Aminotran_5, 1 hit
PIRSFⁱ	PIRSF005572 NifS, 1 hit
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
TIGRFAMsⁱ	TIGR02006 IscS, 1 hit
PROSITEⁱ	View protein in PROSITE PS00595 AA_TRANSFER_CLASS_5, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ISCS_ECOLI
Accessionⁱ	P0A6B7Primary (citable) accession number: P0A6B7 Secondary accession number(s): P39171 , P76581, P76992, Q8XA86
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
	Last sequence update:	June 7, 2005
	Last modified:	November 7, 2018
	This is version 123 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, Direct protein sequencing, 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 - P0A6B7 (ISCS_ECOLI)

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Cysteine desulfurase IscS

iscS

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

<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: iron-sulfur cluster biosynthesis

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

Keywords - 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

<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

Amino acid modifications

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

<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

Experimental Info

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

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

Pathwayⁱ: iron-sulfur cluster biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ