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UniProtKB - P0A6B7 (ISCS_ECOLI)

>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

Entry version 144 (25 May 2022)
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

[sulfur carrier]-H
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+
L-cysteine
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See the description of this molecule in ChEBI.
=
[sulfur carrier]-SH
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+
L-alanine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00331
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase."
  Flint D.H.
  J. Biol. Chem. 271:16068-16074(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 1-38; 43-66; 117-127; 212-219; 241-257; 319-339 AND 382-391, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE.
EC:
2.8.1.7
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00331
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase."
  Flint D.H.
  J. Biol. Chem. 271:16068-16074(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 1-38; 43-66; 117-127; 212-219; 241-257; 319-339 AND 382-391, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
[sulfur carrier]-H
H group
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+
L-cysteine
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=
[sulfur carrier]-SH
thiol group
zoom
+
L-alanine
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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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

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
SABIO-RKⁱ	P0A6B7
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

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

jPOSTⁱ	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

Hide details

P0A6B7

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

Protein-protein interaction databases

BioGRIDⁱ	4263511, 579 interactors 851343, 3 interactors
ComplexPortalⁱ	CPX-2136, L-cysteine desulfurase complex CPX-2139, iscS-tusA cysteine desulfurase complex CPX-2140, iscS-thiI sulfurtransferase complex CPX-2141, iscS-iscU iron-sulfur cluster assembly complex
Database of interacting proteins More...DIPⁱ	DIP-29109N
IntActⁱ	P0A6B7, 47 interactors
Molecular INTeraction database More...MINTⁱ	P0A6B7
STRINGⁱ	511145.b2530

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

AlphaFoldDBⁱ	P0A6B7
SASBDBⁱ	P0A6B7
SMRⁱ	P0A6B7
ModBaseⁱ	Search...
PDBe-KBⁱ	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	COG1104, Bacteria
HOGENOMⁱ	CLU_003433_0_2_6
InParanoidⁱ	P0A6B7
OMAⁱ	KGLYWAR
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 IPR015421, PyrdxlP-dep_Trfase_major IPR015422, PyrdxlP-dep_Trfase_small
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

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        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_STEB01000011.1 YP_026169.1, NC_000913.3

Genome annotation databases

EnsemblBacteriaⁱ	AAT48142; AAT48142; b2530 BAA16424; BAA16424; BAA16424
GeneIDⁱ	67416914 947004
KEGGⁱ	ecj:JW2514 eco:b2530
PATRICⁱ	fig\|1411691.4.peg.4204

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

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
+209

Protein	Similar proteins		Species	Score	Length	Source
P0A6B7	Cysteine desulfurase IscS		PECAS		404	UniRef90_Q6D259
Cysteine desulfurase IscS		SALSV		404
Cysteine desulfurase IscS		SALPC		404
Cysteine desulfurase IscS		ESCF3		404
Cysteine desulfurase IscS		PHOLL		404
+1917

Protein	Similar proteins		Species	Score	Length	Source
P0A6B7	Cysteine desulfurase IscS		AZOVI		404	UniRef50_O31269
Cysteine desulfurase IscS		AZOVD		404
Cysteine desulfurase IscS		SHEPW		404
Cysteine desulfurase IscS		SHEPA		404
Cysteine desulfurase IscS		ACIBS		405
+10433

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_STEB01000011.1 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	[»]
AlphaFoldDBⁱ	P0A6B7
SASBDBⁱ	P0A6B7
SMRⁱ	P0A6B7
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	4263511, 579 interactors 851343, 3 interactors
ComplexPortalⁱ	CPX-2136, L-cysteine desulfurase complex CPX-2139, iscS-tusA cysteine desulfurase complex CPX-2140, iscS-thiI sulfurtransferase complex CPX-2141, iscS-iscU iron-sulfur cluster assembly complex
DIPⁱ	DIP-29109N
IntActⁱ	P0A6B7, 47 interactors
MINTⁱ	P0A6B7
STRINGⁱ	511145.b2530

Proteomic databases

jPOSTⁱ	P0A6B7
PaxDbⁱ	P0A6B7
PRIDEⁱ	P0A6B7

Genome annotation databases

EnsemblBacteriaⁱ	AAT48142; AAT48142; b2530 BAA16424; BAA16424; BAA16424
GeneIDⁱ	67416914 947004
KEGGⁱ	ecj:JW2514 eco:b2530
PATRICⁱ	fig\|1411691.4.peg.4204

Organism-specific databases

EchoBASEⁱ	EB2542

EchoBASEⁱ

EB2542

Phylogenomic databases

eggNOGⁱ	COG1104, Bacteria
HOGENOMⁱ	CLU_003433_0_2_6
InParanoidⁱ	P0A6B7
OMAⁱ	KGLYWAR
PhylomeDBⁱ	P0A6B7

Enzyme and pathway databases

UniPathwayⁱ	UPA00266
BioCycⁱ	EcoCyc:G7325-MONOMER
SABIO-RKⁱ	P0A6B7

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 IPR015421, PyrdxlP-dep_Trfase_major IPR015422, PyrdxlP-dep_Trfase_small
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
MobiDBⁱ	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:	May 25, 2022
	This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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%5Fsection">'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

<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

Cytoplasm and Cytosol

Cytosol

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

P0A6B7

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

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

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Pathwayⁱ: iron-sulfur cluster biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ