UniProtKB - P24182 (ACCC_ECOLI)

BLAST

>sp|P24182|ACCC_ECOLI Biotin carboxylase OS=Escherichia coli (strain K12) OX=83333 GN=accC PE=1 SV=2
MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSY
LNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAI
AAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQ
SISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV
EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVT
EMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAP
GGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDL
QIRIMNDENFQHGGTNIHYLEKKLGLQEK

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History
Entry version 181 (07 Nov 2018)
Sequence version 2 (01 Feb 1994)
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Protein

Biotin carboxylase

Gene

accC

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.

Catalytic activityⁱ

ATP + [biotin carboxyl-carrier protein]-biotin-N₆-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N₆-L-lysine.

ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA.

Pathwayⁱ: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Biotin carboxylase (accC), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA)

This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	116	ATP1 Publication	1
Binding siteⁱ	201	ATP1 Publication	1
Binding siteⁱ	236	ATP1 Publication	1
Active siteⁱ	292	Sequence analysis	1

GO - Molecular functionⁱ

acetyl-CoA carboxylase activity Source: UniProtKB-EC
ATP binding Source: UniProtKB-KW
biotin carboxylase activity
Source: EcoliWiki
Inferred from direct assayⁱ
- 10893421
metal ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

fatty acid biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 10893421
malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
negative regulation of fatty acid biosynthetic process
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 17056747

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Ligase
Biological process	Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
Ligand	ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:BIOTIN-CARBOXYL-MONOMER MetaCyc:BIOTIN-CARBOXYL-MONOMER
BRENDAⁱ	6.3.4.14 2026
SABIO-RKⁱ	P24182
UniPathwayⁱ	UPA00655;UER00711

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Biotin carboxylase (EC:6.3.4.14) Alternative name(s): Acetyl-CoA carboxylase subunit A (EC:6.4.1.2) Short name: ACC
Gene namesⁱ	Name:accC Synonyms:fabG Ordered Locus Names:b3256, JW3224
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	EG10276 accC

EcoGeneⁱ

EG10276 accC

Subcellular locationⁱ

GO - Cellular componentⁱ

cytoplasm
Source: EcoliWiki
Inferred by curatorⁱ
- 10893421
cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	19	R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication	1
Mutagenesisⁱ	23	E → R: Loss of homodimerization. No effect on ATP binding. 1 Publication	1
Mutagenesisⁱ	363	F → A: Loss of homodimerization. No effect on ATP binding. 1 Publication	1
Mutagenesisⁱ	366	R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB08074 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine

DrugBankⁱ

DB08074 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000146791	1 – 449	Biotin carboxylaseAdd BLAST		449

Proteomic databases

EPDⁱ	P24182
PaxDbⁱ	P24182
PRIDEⁱ	P24182

Interactionⁱ

Subunit structureⁱ

Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex.2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
accB	P0ABD8	10	EBI-542308,EBI-542320
accD	P0A9Q5	4	EBI-542308,EBI-542064
cysM	P16703	3	EBI-542308,EBI-542376
ribD	P25539	3	EBI-542308,EBI-552457

Protein-protein interaction databases

BioGridⁱ	4262456, 269 interactors
ComplexPortalⁱ	CPX-3206 Acetyl-CoA carboxylase complex
Database of interacting proteins More...DIPⁱ	DIP-9035N
IntActⁱ	P24182, 20 interactors
STRINGⁱ	316385.ECDH10B_3431

Chemistry databases

BindingDBⁱ

P24182

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 7	Combined sources	5
Helixⁱ	11 – 24	Combined sources	14
Beta strandⁱ	27 – 33	Combined sources	7
Helixⁱ	34 – 36	Combined sources	3
Helixⁱ	40 – 44	Combined sources	5
Beta strandⁱ	45 – 52	Combined sources	8
Helixⁱ	56 – 58	Combined sources	3
Turnⁱ	59 – 61	Combined sources	3
Helixⁱ	63 – 73	Combined sources	11
Beta strandⁱ	77 – 79	Combined sources	3
Turnⁱ	84 – 87	Combined sources	4
Helixⁱ	89 – 97	Combined sources	9
Beta strandⁱ	101 – 105	Combined sources	5
Helixⁱ	107 – 114	Combined sources	8
Helixⁱ	116 – 126	Combined sources	11
Helixⁱ	142 – 152	Combined sources	11
Beta strandⁱ	154 – 160	Combined sources	7
Turnⁱ	165 – 168	Combined sources	4
Beta strandⁱ	170 – 172	Combined sources	3
Helixⁱ	175 – 193	Combined sources	19
Beta strandⁱ	198 – 202	Combined sources	5
Beta strandⁱ	208 – 216	Combined sources	9
Beta strandⁱ	218 – 220	Combined sources	3
Beta strandⁱ	222 – 234	Combined sources	13
Beta strandⁱ	237 – 244	Combined sources	8
Helixⁱ	250 – 267	Combined sources	18
Beta strandⁱ	271 – 280	Combined sources	10
Beta strandⁱ	283 – 290	Combined sources	8
Helixⁱ	297 – 304	Combined sources	8
Helixⁱ	308 – 317	Combined sources	10
Helixⁱ	325 – 327	Combined sources	3
Beta strandⁱ	332 – 340	Combined sources	9
Turnⁱ	344 – 346	Combined sources	3
Beta strandⁱ	356 – 358	Combined sources	3
Beta strandⁱ	365 – 368	Combined sources	4
Beta strandⁱ	379 – 381	Combined sources	3
Beta strandⁱ	383 – 394	Combined sources	12
Helixⁱ	395 – 408	Combined sources	14
Beta strandⁱ	410 – 414	Combined sources	5
Helixⁱ	418 – 425	Combined sources	8
Helixⁱ	428 – 432	Combined sources	5
Helixⁱ	439 – 444	Combined sources	6

Show more details

3D structure databases

ProteinModelPortalⁱ	P24182
SMRⁱ	P24182
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P24182

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 445	Biotin carboxylationAdd BLAST		445
Domainⁱ	120 – 317	ATP-graspPROSITE-ProRule annotationAdd BLAST		198

Phylogenomic databases

eggNOGⁱ	ENOG4105CER Bacteria COG0439 LUCA
HOGENOMⁱ	HOG000008988
InParanoidⁱ	P24182
KEGG Orthology (KO) More...KOⁱ	K01961
PhylomeDBⁱ	P24182

Family and domain databases

Gene3Dⁱ	3.30.1490.20, 1 hit
InterProⁱ	View protein in InterPro IPR004549 Acetyl_CoA_COase_biotin_COase IPR011761 ATP-grasp IPR013815 ATP_grasp_subdomain_1 IPR005481 BC-like_N IPR011764 Biotin_carboxylation_dom IPR005482 Biotin_COase_C IPR005479 CbamoylP_synth_lsu-like_ATP-bd IPR016185 PreATP-grasp_dom_sf IPR011054 Rudment_hybrid_motif
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02785 Biotin_carb_C, 1 hit PF00289 Biotin_carb_N, 1 hit PF02786 CPSase_L_D2, 1 hit
SMARTⁱ	View protein in SMART SM00878 Biotin_carb_C, 1 hit
SUPFAMⁱ	SSF51246 SSF51246, 1 hit SSF52440 SSF52440, 1 hit
TIGRFAMsⁱ	TIGR00514 accC, 1 hit
PROSITEⁱ	View protein in PROSITE PS50975 ATP_GRASP, 1 hit PS50979 BC, 1 hit PS00866 CPSASE_1, 1 hit PS00867 CPSASE_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P24182-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC 
        60         70         80         90        100
IGPAPSVKSY LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF 
       110        120        130        140        150
IFIGPKAETI RLMGDKVSAI AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK 
       160        170        180        190        200
RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ SISMTRAEAK AAFSNDMVYM 
       210        220        230        240        250
EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV EEAPAPGITP 
       260        270        280        290        300
ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 
       310        320        330        340        350
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS 
       360        370        380        390        400
PGKITRFHAP GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA 
       410        420        430        440 
RMKNALQELI IDGIKTNVDL QIRIMNDENF QHGGTNIHYL EKKLGLQEK

Length:449

Mass (Da):49,321

Last modified:February 1, 1994 - v2

Checksum:ⁱ68C55F10ACB4F170

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	136	G → A (PubMed:2575489).Curated	1
Sequence conflictⁱ	160	A → P (PubMed:2575489).Curated	1
Sequence conflictⁱ	260 – 261	CA → SR (PubMed:1370469).Curated	2
Sequence conflictⁱ	313	L → M in AAA23748 (PubMed:1682920).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M79446 Genomic DNA Translation: AAA23748.1 M80458 Genomic DNA Translation: AAA23409.1 M83198 Genomic DNA Translation: AAA23746.1 U18997 Genomic DNA Translation: AAA58059.1 U00096 Genomic DNA Translation: AAC76288.1 AP009048 Genomic DNA Translation: BAE77297.1 M32214 Genomic DNA No translation available.
PIRⁱ	JS0632
NCBI Reference Sequences More...RefSeqⁱ	NP_417722.1, NC_000913.3 WP_000884639.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76288; AAC76288; b3256 BAE77297; BAE77297; BAE77297
GeneIDⁱ	947761
KEGGⁱ	ecj:JW3224 eco:b3256
PATRICⁱ	fig\|511145.12.peg.3355

Protein	Similar proteins		Species	Score	Length	Source
P24182	Biotin carboxylase		TRITR		449	UniRef100_P24182
Acetyl-CoA carboxylase biotin carboxylase subunit		Shigella sp.		449
Biotin carboxylase		Escherichia coli O145 str. RM9872		449
Biotin carboxylase		Klebsiella pneumoniae IS22		449
Biotin carboxylase		KLEPN		449
+134

Protein	Similar proteins		Species	Score	Length	Source
P24182	Biotin carboxylase		TRITR		449	UniRef90_P24182
Acetyl-CoA carboxylase biotin carboxylase subunit		Shigella sp.		449
Biotin carboxylase		Escherichia coli O145 str. RM9872		449
Biotin carboxylase		Klebsiella pneumoniae IS22		449
Biotin carboxylase		KLEPN		449
+512

Protein	Similar proteins		Species	Score	Length	Source
P24182	Biotin carboxylase		NOSS1		447	UniRef50_P24182
Biotin carboxylase		ECO57		449
Biotin carboxylase		TRITR		449
Acetyl-CoA carboxylase biotin carboxylase subunit		Shigella sp.		449
Biotin carboxylase		Escherichia coli O145 str. RM9872		449
+1785

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M79446 Genomic DNA Translation: AAA23748.1 M80458 Genomic DNA Translation: AAA23409.1 M83198 Genomic DNA Translation: AAA23746.1 U18997 Genomic DNA Translation: AAA58059.1 U00096 Genomic DNA Translation: AAC76288.1 AP009048 Genomic DNA Translation: BAE77297.1 M32214 Genomic DNA No translation available.
PIRⁱ	JS0632
RefSeqⁱ	NP_417722.1, NC_000913.3 WP_000884639.1, 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
	1BNC	X-ray	2.40	A/B	1-449	[»]
	1DV1	X-ray	1.90	A/B	1-449	[»]
	1DV2	X-ray	2.50	A/B	1-449	[»]
	1K69	model	-	A	1-447	[»]
	2GPS	X-ray	2.80	A/B	1-449	[»]
	2GPW	X-ray	2.20	A/B/C/D	1-449	[»]
	2J9G	X-ray	2.05	A/B	1-449	[»]
	2V58	X-ray	2.10	A/B	1-449	[»]
	2V59	X-ray	2.40	A/B	1-449	[»]
	2V5A	X-ray	2.31	A/B	1-449	[»]
	2VR1	X-ray	2.60	A/B	1-449	[»]
	2W6M	X-ray	2.00	A/B	1-449	[»]
	2W6N	X-ray	1.87	A/B	1-449	[»]
	2W6O	X-ray	2.50	A/C	1-449	[»]
	2W6P	X-ray	1.85	A/B	1-449	[»]
	2W6Q	X-ray	2.05	A/B	1-449	[»]
	2W6Z	X-ray	1.90	A/B	1-449	[»]
	2W70	X-ray	1.77	A/B	1-449	[»]
	2W71	X-ray	1.99	A/C	1-449	[»]
	3G8C	X-ray	2.00	A/B	1-444	[»]
	3G8D	X-ray	1.90	A/B	1-444	[»]
	3JZF	X-ray	2.13	A/B	1-449	[»]
	3JZI	X-ray	2.31	A/B	1-449	[»]
	3RUP	X-ray	1.99	A/B	1-449	[»]
	3RV3	X-ray	1.91	A/B	1-449	[»]
	3RV4	X-ray	1.98	A	1-449	[»]
	4HR7	X-ray	2.50	A/C/E/F	1-449	[»]
ProteinModelPortalⁱ	P24182
SMRⁱ	P24182
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262456, 269 interactors
ComplexPortalⁱ	CPX-3206 Acetyl-CoA carboxylase complex
DIPⁱ	DIP-9035N
IntActⁱ	P24182, 20 interactors
STRINGⁱ	316385.ECDH10B_3431

Chemistry databases

BindingDBⁱ	P24182
DrugBankⁱ	DB08074 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine

Proteomic databases

EPDⁱ	P24182
PaxDbⁱ	P24182
PRIDEⁱ	P24182

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76288; AAC76288; b3256 BAE77297; BAE77297; BAE77297
GeneIDⁱ	947761
KEGGⁱ	ecj:JW3224 eco:b3256
PATRICⁱ	fig\|511145.12.peg.3355

Organism-specific databases

EchoBASEⁱ	EB0272
EcoGeneⁱ	EG10276 accC

Phylogenomic databases

eggNOGⁱ	ENOG4105CER Bacteria COG0439 LUCA
HOGENOMⁱ	HOG000008988
InParanoidⁱ	P24182
KOⁱ	K01961
PhylomeDBⁱ	P24182

Enzyme and pathway databases

UniPathwayⁱ	UPA00655;UER00711
BioCycⁱ	EcoCyc:BIOTIN-CARBOXYL-MONOMER MetaCyc:BIOTIN-CARBOXYL-MONOMER
BRENDAⁱ	6.3.4.14 2026
SABIO-RKⁱ	P24182

Miscellaneous databases

EvolutionaryTraceⁱ	P24182
Protein Ontology More...PROⁱ	PR:P24182

Family and domain databases

Gene3Dⁱ	3.30.1490.20, 1 hit
InterProⁱ	View protein in InterPro IPR004549 Acetyl_CoA_COase_biotin_COase IPR011761 ATP-grasp IPR013815 ATP_grasp_subdomain_1 IPR005481 BC-like_N IPR011764 Biotin_carboxylation_dom IPR005482 Biotin_COase_C IPR005479 CbamoylP_synth_lsu-like_ATP-bd IPR016185 PreATP-grasp_dom_sf IPR011054 Rudment_hybrid_motif
Pfamⁱ	View protein in Pfam PF02785 Biotin_carb_C, 1 hit PF00289 Biotin_carb_N, 1 hit PF02786 CPSase_L_D2, 1 hit
SMARTⁱ	View protein in SMART SM00878 Biotin_carb_C, 1 hit
SUPFAMⁱ	SSF51246 SSF51246, 1 hit SSF52440 SSF52440, 1 hit
TIGRFAMsⁱ	TIGR00514 accC, 1 hit
PROSITEⁱ	View protein in PROSITE PS50975 ATP_GRASP, 1 hit PS50979 BC, 1 hit PS00866 CPSASE_1, 1 hit PS00867 CPSASE_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACCC_ECOLI
Accessionⁱ	P24182Primary (citable) accession number: P24182 Secondary accession number(s): Q2M8V9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
	Last sequence update:	February 1, 1994
	Last modified:	November 7, 2018
	This is version 181 of the entry and version 2 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

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

UniProtKB

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Supporting data

UniProtKB - P24182 (ACCC_ECOLI)

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Biotin carboxylase

accC

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_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: malonyl-CoA 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

<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

Domains and Repeats

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

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

UniProt is an ELIXIR core data resource

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Functionⁱ

Pathwayⁱ: malonyl-CoA biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ