P44458 (CITXG_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein CitXG

Including the following 2 domains:

1. Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase
   EC=2.7.7.61
   Alternative name(s):
   Apo-ACP nucleodityltransferase
   Holo-ACP synthase
   Holo-citrate lyase synthase
2. 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase
   Short name=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase
   EC=2.7.8.25

Gene names

Name:	citXG
Synonyms:	citG
Ordered Locus Names:	HI_0021

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, and then the transfer of this prosthetic group precursor to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield the holo-acyl carrier protein By similarity. HAMAP MF_00397
Catalytic activity	2'-(5-triphosphoribosyl)-3'-dephospho-CoA + citrate lyase apo-[acyl-carrier-protein] = citrate lyase holo-[acyl-carrier-protein] + diphosphate. HAMAP MF_00397 ATP + 3-dephospho-CoA = 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + adenine. HAMAP MF_00397
Sequence similarities	In the N-terminal section; belongs to the CitX family. In the C-terminal section; belongs to the CitG/MdcB family.
Sequence caution	The sequence AAC21699.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	phosphorylation Inferred from electronic annotation. Source: InterPro prosthetic group biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW holo-citrate lyase synthase activity Inferred from electronic annotation. Source: EC triphosphoribosyl-dephospho-CoA synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 465	465	Protein CitXG HAMAP MF_00397		PRO_0000214682
Regions
	Region	1 – 182	182	Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase HAMAP MF_00397
	Region	183 – 465	283	2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase HAMAP MF_00397

Sequences

	Sequence		Length	Mass (Da)
	P44458 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: 4467221C3DB58A96	FASTA	465	51,835
	10 20 30 40 50 60 MQHFFTTFST EGSKISLEAL LNAREERAIL QQQLITQYGQ TLLCITLTAM GGVKKNALLD 70 80 90 100 110 120 YVFTKALENL TALFTQLNIT AVKEIIRPLE TGHEAYFVLP IDARTLKVLM IELEESIPLA 130 140 150 160 170 180 RLWDLDVFNA KGNLLSRTDF DLSPRTCLVC GENAKICART HKHEIDEIVD KIQSLAQNHD 190 200 210 220 230 240 FAEHIGEQVY LALIQEARLS PKPGLVDAIN NGSHKDMNLH TFEQSAISLK PFFTQFVLKG 250 260 270 280 290 300 MMTAHLSENQ ILSEIRPLGL LAEKAMFKVT DGVNTHKGAI FSFGLVCTAI GRLLAQKSLV 310 320 330 340 350 360 QSAVDFDVKL ICSLVAQFTQ GLTDELKNYP EHLPSTAGVR LFQKYGLTGV RGEAENGFNL 370 380 390 400 410 420 IQTLLPQFDE YHQLEWEHRL LILLLNLMAI NSDTNVVHRG GLAGLYFIQQ TAQDLLTDQH 430 440 450 460 LVTDKTALTQ ALMKFDTACI ERNLSSGGSA DLLALTIFFL SFRGN

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC21699.1. Different initiation.
PIR	E64140.
RefSeq	NP_438194.1. NC_000907.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	950919.
GenomeReviews	Gene locus HI_0021 in contig L42023_GR.
KEGG	hin:HI0021.
NMPDR	fig|71421.1.peg.20.
PATRIC	20188493. VBIHaeInf48452_0021.
TIGR	HI_0021.
Phylogenomic databases
HOGENOM	HBG305005.
OMA	TGHEAFF.
ProtClustDB	CLSK892351.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0021-MONOMER.
Family and domain databases
HAMAP	MF_00397. CitG. Fused. [Tree] MF_00398. CitX. Fused. [Tree]
InterPro	IPR002736. CitG. IPR005551. CitX. IPR017551. TriPribosyl-deP-CoA_syn_CitG. [Graphical view]
KO	K13927.
Pfam	PF01874. CitG. 1 hit. PF03802. CitX. 1 hit. [Graphical view]
TIGRFAMs	TIGR03125. Citrate_citG. 1 hit. TIGR03124. Citrate_citX. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CITXG_HAEIN

Accession

Primary (citable) accession number: P44458

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program