P77231 (CITG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase
Short name=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase
EC=2.7.8.25

Gene names

Name:	citG
Synonyms:	ybdT
Ordered Locus Names:	b0613, JW0605

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA. Ref.4 Ref.5
Catalytic activity	ATP + 3-dephospho-CoA = 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + adenine. HAMAP-Rule MF_00397
Induction	Repressed by H-NS. Part of the citCDEFXG operon. Ref.6
Sequence similarities	Belongs to the CitG/MdcB family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW triphosphoribosyl-dephospho-CoA synthase activity 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 – 292	292	2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase HAMAP-Rule MF_00397		PRO_0000214664

Sequences

	Sequence		Length	Mass (Da)
	P77231 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 0BE3C24BE33E0AE8	FASTA	292	31,644
	10 20 30 40 50 60 MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH KDMALEDFHR 70 80 90 100 110 120 SALAIQGWLP RFIEFGACSA EMAPEAVLHG LRPIGMACEG DMFRATAGVN THKGSIFSLG 130 140 150 160 170 180 LLCAAIGRLL QLNQPVTPTT VCSTAASFCR GLTDRELRTN NSQLTAGQRL YQQLGLTGAR 190 200 210 220 230 240 GEAEAGYPLV INHALPHYLT LLDQGLDPEL ALLDTLLLLM AINGDTNVAS RGGEGGLRWL 250 260 270 280 290 QREAQTLLQK GGIRTPADLD YLRQFDRECI ERNLSPGGSA DLLILTWFLA QI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group." Schneider K., Dimroth P., Bott M. FEBS Lett. 483:165-168(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Biosynthesis of the prosthetic group of citrate lyase." Schneider K., Dimroth P., Bott M. Biochemistry 39:9438-9450(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: BL21-DE3 and K12 / DH5-alpha.
[6]	"Involvement of the leucine response transcription factor LeuO in regulation of the genes for sulfa drug efflux." Shimada T., Yamamoto K., Ishihama A. J. Bacteriol. 191:4562-4571(2009) [PubMed] [Europe PMC] [Abstract] Cited for: OPERON STRUCTURE, INDUCTION. Strain: K12 / BW25113.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U82598 Genomic DNA. Translation: AAB40813.1. U00096 Genomic DNA. Translation: AAC73714.1. AP009048 Genomic DNA. Translation: BAE76353.1.
PIR	C64795.
RefSeq	NP_415146.1. NC_000913.2. YP_488902.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P77231.
ModBase	Search...
Protein-protein interaction databases
IntAct	P77231. 2 interactions.
STRING	511145.b0613.
Proteomic databases
PaxDb	P77231.
PRIDE	P77231.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73714; AAC73714; b0613. BAE76353; BAE76353; BAE76353.
GeneID	12930909. 946395.
KEGG	ecj:Y75_p0602. eco:b0613.
PATRIC	32116406. VBIEscCol129921_0643.
Organism-specific databases
EchoBASE	EB3309.
EcoGene	EG13539. citG.
Phylogenomic databases
eggNOG	COG1767.
HOGENOM	HOG000258582.
KO	K05966.
OMA	DPESNGA.
ProtClustDB	PRK10096.
Enzyme and pathway databases
BioCyc	EcoCyc:G6339-MONOMER. ECOL316407:JW0605-MONOMER. MetaCyc:G6339-MONOMER.
Gene expression databases
Genevestigator	P77231.
Family and domain databases
HAMAP	MF_00397. CitG.
InterPro	IPR002736. CitG. IPR017551. TriPribosyl-deP-CoA_syn_CitG. [Graphical view]
Pfam	PF01874. CitG. 1 hit. [Graphical view]
TIGRFAMs	TIGR03125. citrate_citG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CITG_ECOLI

Accession

Primary (citable) accession number: P77231
Secondary accession number(s): Q2MBK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program