Q58787 (CIMA_METJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
(R)-citramalate synthase CimA
EC=2.3.1.182

Gene names

Name:	cimA
Ordered Locus Names:	MJ1392

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate. Ref.2
Catalytic activity	Acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate. Ref.2
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3. Ref.2
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the alpha-IPM synthase/homocitrate synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Inferred from electronic annotation. Source: HAMAP leucine biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	(R)-citramalate synthase activity Inferred from electronic annotation. Source: InterPro 2-isopropylmalate synthase activity Inferred from electronic annotation. Source: InterPro transferase activity, transferring acyl groups other than amino-acyl groups Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 491	491	(R)-citramalate synthase CimA HAMAP-Rule MF_01028		PRO_0000140450
Experimental info
	Sequence conflict	2	1	M → L AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q58787 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 9D4FA0EA6F8F3BE5	FASTA	491	53,493
	10 20 30 40 50 60 MMVRIFDTTL RDGEQTPGVS LTPNDKLEIA KKLDELGVDV IEAGSAITSK GEREGIKLIT 70 80 90 100 110 120 KEGLNAEICS FVRALPVDID AALECDVDSV HLVVPTSPIH MKYKLRKTED EVLETALKAV 130 140 150 160 170 180 EYAKEHGLIV ELSAEDATRS DVNFLIKLFN EGEKVGADRV CVCDTVGVLT PQKSQELFKK 190 200 210 220 230 240 ITENVNLPVS VHCHNDFGMA TANTCSAVLG GAVQCHVTVN GIGERAGNAS LEEVVAALKI 250 260 270 280 290 300 LYGYDTKIKM EKLYEVSRIV SRLMKLPVPP NKAIVGDNAF AHEAGIHVDG LIKNTETYEP 310 320 330 340 350 360 IKPEMVGNRR RIILGKHSGR KALKYKLDLM GINVSDEQLN KIYERVKEFG DLGKYISDAD 370 380 390 400 410 420 LLAIVREVTG KLVEEKIKLD ELTVVSGNKI TPIASVKLHY KGEDITLIET AYGVGPVDAA 430 440 450 460 470 480 INAVRKAISG VADIKLVEYR VEAIGGGTDA LIEVVVKLRK GTEIVEVRKS DADIIRASVD 490 AVMEGINMLL N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"(R)-citramalate synthase in methanogenic archaea." Howell D.M., Xu H., White R.H. J. Bacteriol. 181:331-333(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB99402.1.
PIR	G64473.
RefSeq	NP_248395.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58787.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ1392.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB99402; AAB99402; MJ_1392.
GeneID	1452295.
KEGG	mja:MJ_1392.
Phylogenomic databases
eggNOG	COG0119.
KO	K09011.
OMA	GARTDII.
ProtClustDB	PRK09389.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11899.
UniPathway	UPA00047; UER00066.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01028. CimA.
InterPro	IPR013709. 2-isopropylmalate_synth_dimer. IPR002034. AIPM/Hcit_synth_CS. IPR013785. Aldolase_TIM. IPR024890. Citramalate_synthase_CimA. IPR011830. LEU1_arch. IPR000891. PYR_CT. [Graphical view]
Pfam	PF00682. HMGL-like. 1 hit. PF08502. LeuA_dimer. 1 hit. [Graphical view]
SMART	SM00917. LeuA_dimer. 1 hit. [Graphical view]
SUPFAM	SSF110921. 2-isopropylmalate_synth_dimer. 1 hit.
TIGRFAMs	TIGR02090. LEU1_arch. 1 hit.
PROSITE	PS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit. PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit. PS50991. PYR_CT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CIMA_METJA

Accession

Primary (citable) accession number: Q58787

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program