cimA

Functionⁱ

Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate (PubMed:15292141, PubMed:18498255, PubMed:19351325).

Shows strict substrate specificity for pyruvate. Cannot use alpha-ketoisovalerate, alpha-ketobutyrate, alpha-ketoisocaproate, alpha-ketoglutarate or glyoxylate (PubMed:15292141, PubMed:18498255).

3 Publications

Catalytic activityⁱ

acetyl-CoA
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See the description of this molecule in ChEBI.
+
H₂O
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See the description of this molecule in ChEBI.
+
pyruvate
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See the description of this molecule in ChEBI.
=
(3R)-citramalate
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
CoA
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See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway."
  Xu H., Zhang Y., Guo X., Ren S., Staempfli A.A., Chiao J., Jiang W., Zhao G.
  J. Bacteriol. 186:5400-5409(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INDUCTION.
- Ref.3
  "Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans."
  Ma J., Zhang P., Zhang Z., Zha M., Xu H., Zhao G., Ding J.
  Biochem. J. 415:45-56(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-325 IN COMPLEXES WITH PYRUVATE; ACETYL-COA; MALONATE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, ACTIVE SITE, MUTAGENESIS OF ARG-16; ASP-17; LEU-81; PHE-83; LEU-104; TYR-144; GLU-146; THR-179; HIS-302; ASP-304; ASN-310; LEU-311 AND TYR-312.
- Ref.4
  "Molecular basis of the inhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from Leptospira interrogans."
  Zhang P., Ma J., Zhang Z., Zha M., Xu H., Zhao G., Ding J.
  Biochem. J. 421:133-143(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 390-516 IN COMPLEXES WITH ZINC AND ISOLEUCINE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, DOMAIN, MUTAGENESIS OF TYR-430; ASP-431; LEU-451; TYR-454; ILE-458; THR-464; VAL-468; PRO-493 AND GLN-495.
EC:
2.3.1.182
- 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.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway."
  Xu H., Zhang Y., Guo X., Ren S., Staempfli A.A., Chiao J., Jiang W., Zhao G.
  J. Bacteriol. 186:5400-5409(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INDUCTION.
- Ref.3
  "Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans."
  Ma J., Zhang P., Zhang Z., Zha M., Xu H., Zhao G., Ding J.
  Biochem. J. 415:45-56(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-325 IN COMPLEXES WITH PYRUVATE; ACETYL-COA; MALONATE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, ACTIVE SITE, MUTAGENESIS OF ARG-16; ASP-17; LEU-81; PHE-83; LEU-104; TYR-144; GLU-146; THR-179; HIS-302; ASP-304; ASN-310; LEU-311 AND TYR-312.
- Ref.4
  "Molecular basis of the inhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from Leptospira interrogans."
  Zhang P., Ma J., Zhang Z., Zha M., Xu H., Zhao G., Ding J.
  Biochem. J. 421:133-143(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 390-516 IN COMPLEXES WITH ZINC AND ISOLEUCINE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, DOMAIN, MUTAGENESIS OF TYR-430; ASP-431; LEU-451; TYR-454; ILE-458; THR-464; VAL-468; PRO-493 AND GLN-495.
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway."
  Xu H., Zhang Y., Guo X., Ren S., Staempfli A.A., Chiao J., Jiang W., Zhao G.
  J. Bacteriol. 186:5400-5409(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INDUCTION.
- Ref.3
  "Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans."
  Ma J., Zhang P., Zhang Z., Zha M., Xu H., Zhao G., Ding J.
  Biochem. J. 415:45-56(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-325 IN COMPLEXES WITH PYRUVATE; ACETYL-COA; MALONATE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, ACTIVE SITE, MUTAGENESIS OF ARG-16; ASP-17; LEU-81; PHE-83; LEU-104; TYR-144; GLU-146; THR-179; HIS-302; ASP-304; ASN-310; LEU-311 AND TYR-312.
- Ref.4
  "Molecular basis of the inhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from Leptospira interrogans."
  Zhang P., Ma J., Zhang Z., Zha M., Xu H., Zhao G., Ding J.
  Biochem. J. 421:133-143(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 390-516 IN COMPLEXES WITH ZINC AND ISOLEUCINE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, DOMAIN, MUTAGENESIS OF TYR-430; ASP-431; LEU-451; TYR-454; ILE-458; THR-464; VAL-468; PRO-493 AND GLN-495.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
acetyl-CoA
zoom
+
H₂O
+
pyruvate
zoom
=
(3R)-citramalate
zoom
+
CoA
+
H⁺

Cofactorⁱ

Mn²⁺1 PublicationNote: Mn²⁺ is the most effective activator, followed by Co²⁺, Ca²⁺, Mg²⁺ and Ni²⁺.1 Publication

Activity regulationⁱ

Regulated by the end-product isoleucine via a feedback inhibition. The binding of isoleucine has inhibitory effects on the binding of both pyruvate and acetyl-CoA. May act via conformational change of the dimer interface of the regulatory domain, leading to inhibition of the catalytic reaction.1 Publication

Kineticsⁱ

kcat is 2.41 sec(-1) (PubMed:15292141). kcat is 10.3 sec(-1) with acetyl-CoA as substrate (PubMed:18498255). kcat is 9.13 sec(-1) with pyruvate as substrate (PubMed:18498255).2 Publications

Temperature dependenceⁱ

Optimum temperature is 35-40 degrees Celsius.1 Publication

Pathwayⁱ: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 2-oxobutanoate from pyruvate.1 Publication This subpathway is part of the pathway L-isoleucine 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 2-oxobutanoate from pyruvate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	16	Proton donor1 Publication	1
Metal bindingⁱ	17	Manganese2 Publications	1
Binding siteⁱ	144	Pyruvate1 Publication	1
Active siteⁱ	146	Proton acceptor1 Publication	1
Binding siteⁱ	179	Pyruvate1 Publication	1
Metal bindingⁱ	207	Manganese; via tele nitrogen2 Publications	1
Metal bindingⁱ	209	Manganese; via tele nitrogen2 Publications	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase, Transferase
Biological process	Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis
Ligand	Manganese, Metal-binding, Pyruvate

Enzyme and pathway databases

BioCycⁱ	LINT189518:G1GL4-1907-MONOMER MetaCyc:MONOMER-11894
UniPathwayⁱ	UPA00047;UER00066

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: (R)-citramalate synthase CimACurated (EC:2.3.1.1823 Publications) Alternative name(s): LiCMS1 Publication
Gene namesⁱ	Name:cimA1 Publication Ordered Locus Names:LA_2350Imported
Organismⁱ	Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifierⁱ	189518 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Leptospirales › Leptospiraceae › Leptospira › Leptospira interrogans › Leptospira interrogans serovar Lai
Proteomesⁱ	UP000001408 Componentⁱ: Chromosome I

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	16	R → K or Q: Loss of activity. 1 Publication	1
Mutagenesisⁱ	17	D → A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	17	D → N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	81	L → A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	81	L → V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	83	F → A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	104	L → V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	144	Y → L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	144	Y → V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	146	E → D or Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat. 1 Publication	1
Mutagenesisⁱ	179	T → A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	302	H → A or N: Loss of activity. 1 Publication	1
Mutagenesisⁱ	304	D → A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	310	N → A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	311	L → A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	312	Y → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	430	Y → L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine. 1 Publication	1
Mutagenesisⁱ	431	D → A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	451	L → V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat. 1 Publication	1
Mutagenesisⁱ	454	Y → A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine. 1 Publication	1
Mutagenesisⁱ	458	I → A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine. 1 Publication	1
Mutagenesisⁱ	464	T → A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	468	V → A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor. 1 Publication	1
Mutagenesisⁱ	493	P → A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat. 1 Publication	1
Mutagenesisⁱ	495	Q → A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000449424	1 – 516	(R)-citramalate synthase CimAAdd BLAST		516

Expressionⁱ

Inductionⁱ

Expression is repressed by isoleucine but not by leucine.1 Publication

Interactionⁱ

Subunit structureⁱ

Homodimer.

2 Publications

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	9 – 12	Combined sources	4
Helixⁱ	14 – 18	Combined sources	5
Helixⁱ	28 – 40	Combined sources	13
Beta strandⁱ	45 – 51	Combined sources	7
Helixⁱ	58 – 71	Combined sources	14
Helixⁱ	75 – 77	Combined sources	3
Beta strandⁱ	78 – 85	Combined sources	8
Helixⁱ	88 – 96	Combined sources	9
Beta strandⁱ	100 – 106	Combined sources	7
Helixⁱ	109 – 115	Combined sources	7
Helixⁱ	120 – 136	Combined sources	17
Beta strandⁱ	140 – 146	Combined sources	7
Helixⁱ	148 – 154	Combined sources	7
Helixⁱ	156 – 167	Combined sources	12
Beta strandⁱ	172 – 177	Combined sources	6
Helixⁱ	185 – 198	Combined sources	14
Beta strandⁱ	204 – 207	Combined sources	4
Helixⁱ	215 – 224	Combined sources	10
Beta strandⁱ	228 – 233	Combined sources	6
Helixⁱ	234 – 236	Combined sources	3
Beta strandⁱ	238 – 241	Combined sources	4
Helixⁱ	246 – 256	Combined sources	11
Helixⁱ	265 – 267	Combined sources	3
Helixⁱ	268 – 279	Combined sources	12
Turnⁱ	288 – 290	Combined sources	3
Turnⁱ	292 – 295	Combined sources	4
Helixⁱ	318 – 321	Combined sources	4
Beta strandⁱ	392 – 401	Combined sources	10
Beta strandⁱ	408 – 415	Combined sources	8
Beta strandⁱ	418 – 425	Combined sources	8
Helixⁱ	429 – 444	Combined sources	16
Beta strandⁱ	450 – 457	Combined sources	8
Beta strandⁱ	468 – 475	Combined sources	8
Helixⁱ	482 – 484	Combined sources	3
Beta strandⁱ	486 – 494	Combined sources	9
Helixⁱ	495 – 510	Combined sources	16

Show more details

3D structure databases

SMRⁱ	Q8F3Q1
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q8F3Q1

EvolutionaryTraceⁱ

Q8F3Q1

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	8 – 269	Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST		262

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	16 – 17	Pyruvate binding1 Publication		2

Domainⁱ

Contains a catalytic N-terminal domain and a C-terminal regulatory domain, linked together by a flexible region (PubMed:18498255, PubMed:19351325). The catalytic domain consists of a TIM barrel flanked by an extended C-terminal region. The active site is located at the center of the TIM barrel near the C-terminal ends of the beta-strands and is composed of conserved residues of the beta-strands of one subunit and the C-terminal region of the other (PubMed:18498255).2 Publications

Sequence similaritiesⁱ

Belongs to the alpha-IPM synthase/homocitrate synthase family.Curated

Phylogenomic databases

HOGENOMⁱ	CLU_022158_0_1_12
OMAⁱ	DWSNGMR

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013709, 2-isopropylmalate_synth_dimer IPR002034, AIPM/Hcit_synth_CS IPR013785, Aldolase_TIM IPR036230, LeuA_allosteric_dom_sf IPR000891, PYR_CT
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00682, HMGL-like, 1 hit PF08502, LeuA_dimer, 1 hit
SMARTⁱ	View protein in SMART SM00917, LeuA_dimer, 1 hit
SUPFAMⁱ	SSF110921, SSF110921, 1 hit
PROSITEⁱ	View protein in PROSITE PS00815, AIPM_HOMOCIT_SYNTH_1, 1 hit PS50991, PYR_CT, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q8F3Q1-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTKVETRLEI LDVTLRDGEQ TRGVSFSTSE KLNIAKFLLQ KLNVDRVEIA 
        60         70         80         90        100
SARVSKGELE TVQKIMEWAA TEQLTERIEI LGFVDGNKTV DWIKDSGAKV 
       110        120        130        140        150
LNLLTKGSLH HLEKQLGKTP KEFFTDVSFV IEYAIKSGLK INVYLEDWSN 
       160        170        180        190        200
GFRNSPDYVK SLVEHLSKEH IERIFLPDTL GVLSPEETFQ GVDSLIQKYP 
       210        220        230        240        250
DIHFEFHGHN DYDLSVANSL QAIRAGVKGL HASINGLGER AGNTPLEALV 
       260        270        280        290        300
TTIHDKSNSK TNINEIAITE ASRLVEVFSG KRISANRPIV GEDVFTQTAG 
       310        320        330        340        350
VHADGDKKGN LYANPILPER FGRKRSYALG KLAGKASISE NVKQLGMVLS 
       360        370        380        390        400
EVVLQKVLER VIELGDQNKL VTPEDLPFII ADVSGRTGEK VLTIKSCNIH 
       410        420        430        440        450
SGIGIRPHAQ IELEYQGKIH KEISEGDGGY DAFMNALTKI TNRLGISIPK 
       460        470        480        490        500
LIDYEVRIPP GGKTDALVET RITWNKSLDL EEDQTFKTMG VHPDQTVAAV 
       510 
HATEKMLNQI LQPWQI

Length:516

Mass (Da):57,319

Last modified:March 1, 2003 - v1

Checksum:ⁱ4F0DE93214537124

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE010300 Genomic DNA Translation: AAN49549.1
NCBI Reference Sequences More...RefSeqⁱ	NP_712531.1, NC_004342.2 WP_000169689.1, NC_004342.2

Genome annotation databases

EnsemblBacteriaⁱ	AAN49549; AAN49549; LA_2350
KEGGⁱ	lil:LA_2350
PATRICⁱ	fig\|189518.3.peg.2333

Protein	Similar proteins		Species	Score	Length	Source
Q8F3Q1	HMGL-like protein		Leptospira interrogans serovar Pyrogenes str. L0374		516	UniRef100_Q8F3Q1
HMGL-like protein		Leptospira interrogans str. 2006001854		516
Citramalate synthase (Fragment)		Leptospira interrogans serovar Lai		426
+2

Protein	Similar proteins		Species	Score	Length	Source
Q8F3Q1	HMGL-like protein		Leptospira interrogans serovar Pyrogenes str. L0374		516	UniRef90_Q8F3Q1
HMGL-like protein		Leptospira interrogans str. 2006001854		516
Citramalate synthase (Fragment)		Leptospira interrogans serovar Lai		426
HMGL-like protein		Leptospira noguchii str. Cascata		516
HMGL-like protein		Leptospira weilii serovar Ranarum str. ICFT		516
+116

Protein	Similar proteins		Species	Score	Length	Source
Q8F3Q1	HMGL-like protein		Leptospira interrogans serovar Pyrogenes str. L0374		516	UniRef50_Q8F3Q1
HMGL-like protein		Leptospira interrogans str. 2006001854		516
Citramalate synthase (Fragment)		Leptospira interrogans serovar Lai		426
HMGL-like protein		Leptospira interrogans str. UI 12758		516
2-isopropylmalate synthase		LEPIR		516
+2326

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE010300 Genomic DNA Translation: AAN49549.1
RefSeqⁱ	NP_712531.1, NC_004342.2 WP_000169689.1, NC_004342.2

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
	3BLE	X-ray	2.00	A	1-325	[»]
	3BLF	X-ray	2.60	A	1-325	[»]
	3BLI	X-ray	2.50	A	1-325	[»]
	3F6G	X-ray	2.00	A/B	390-516	[»]
	3F6H	X-ray	2.70	A/B	390-516	[»]
SMRⁱ	Q8F3Q1
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAN49549; AAN49549; LA_2350
KEGGⁱ	lil:LA_2350
PATRICⁱ	fig\|189518.3.peg.2333

Phylogenomic databases

HOGENOMⁱ	CLU_022158_0_1_12
OMAⁱ	DWSNGMR

Enzyme and pathway databases

UniPathwayⁱ	UPA00047;UER00066
BioCycⁱ	LINT189518:G1GL4-1907-MONOMER MetaCyc:MONOMER-11894

Miscellaneous databases

EvolutionaryTraceⁱ	Q8F3Q1

EvolutionaryTraceⁱ

Q8F3Q1

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013709, 2-isopropylmalate_synth_dimer IPR002034, AIPM/Hcit_synth_CS IPR013785, Aldolase_TIM IPR036230, LeuA_allosteric_dom_sf IPR000891, PYR_CT
Pfamⁱ	View protein in Pfam PF00682, HMGL-like, 1 hit PF08502, LeuA_dimer, 1 hit
SMARTⁱ	View protein in SMART SM00917, LeuA_dimer, 1 hit
SUPFAMⁱ	SSF110921, SSF110921, 1 hit
PROSITEⁱ	View protein in PROSITE PS00815, AIPM_HOMOCIT_SYNTH_1, 1 hit PS50991, PYR_CT, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CIMA_LEPIN
Accessionⁱ	Q8F3Q1Primary (citable) accession number: Q8F3Q1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 22, 2020
	Last sequence update:	March 1, 2003
	Last modified:	June 2, 2021
	This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

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UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q8F3Q1 (CIMA_LEPIN)

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(R)-citramalate synthase CimA

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

Temperature dependencei

<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: L-isoleucine 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 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

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<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

<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

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

Genome annotation 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

Catalytic activityⁱ

Kineticsⁱ

Temperature dependenceⁱ

Pathwayⁱ: L-isoleucine biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ