O06162 (CITEL_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Citrate lyase subunit beta-like protein
EC=4.1.-.-

Gene names

Name:	citE
Ordered Locus Names:	Rv2498c, MT2573

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in fatty acid biosynthesis Potential.
Cofactor	Binds 1 magnesium ion per subunit.
Subunit structure	Homotrimer. Ref.3
Sequence similarities	Belongs to the HpcH/HpaI aldolase family. Citrate lyase beta subunit-like subfamily.
Caution	This organism lacks the other subunits that are necessary for ATP-independent citrate lyase activity. Even though this protein has clear similarity to citrate lyase beta subunit, it is expected to have a somewhat different enzyme activity.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular aromatic compound metabolic process Inferred from electronic annotation. Source: InterPro oxaloacetate metabolic process Inferred from physical interaction Ref.3. Source: MTBBASE
Cellular component	citrate lyase complex Inferred from electronic annotation. Source: InterPro
Molecular function	citrate (pro-3S)-lyase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from physical interaction Ref.3. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 273

273

Citrate lyase subunit beta-like protein

PRO_0000286388

Sites

Metal binding

112

1

Magnesium

Metal binding

138

1

Magnesium

Binding site

64

1

Substrate

Binding site

112

1

Substrate

Secondary structure

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273

Helix Strand Turn

Details...

Turn

3 – 5

3

Beta strand

8 – 14

7

Helix

18 – 20

3

Helix

21 – 27

7

Beta strand

29 – 36

8

Helix

41 – 43

3

Helix

44 – 53

10

Beta strand

60 – 64

5

Helix

71 – 81

11

Beta strand

87 – 90

4

Helix

96 – 100

5

Turn

101 – 104

4

Beta strand

105 – 111

7

Helix

114 – 118

5

Helix

120 – 125

6

Beta strand

129 – 134

6

Helix

136 – 143

8

Helix

157 – 172

16

Beta strand

176 – 179

4

Helix

188 – 201

14

Beta strand

204 – 210

7

Helix

211 – 213

3

Helix

214 – 220

7

Sequences

	Sequence		Length	Mass (Da)
	O06162 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 5FD8634672FF5C7C	FASTA	273	28,886
	10 20 30 40 50 60 MNLRAAGPGW LFCPADRPER FAKAAAAADV VILDLEDGVA EAQKPAARNA LRDTPLDPER 70 80 90 100 110 120 TVVRINAGGT ADQARDLEAL AGTAYTTVML PKAESAAQVI ELAPRDVIAL VETARGAVCA 130 140 150 160 170 180 AEIAAADPTV GMMWGAEDLI ATLGGSSSRR ADGAYRDVAR HVRSTILLAA SAFGRLALDA 190 200 210 220 230 240 VHLDILDVEG LQEEARDAAA VGFDVTVCIH PSQIPVVRKA YRPSHEKLAW ARRVLAASRS 250 260 270 ERGAFAFEGQ MVDSPVLTHA ETMLRRAGEA TSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function." Goulding C.W., Bowers P.M., Segelke B., Lekin T., Kim C.Y., Terwilliger T.C., Eisenberg D. J. Mol. Biol. 365:275-283(2007) [PubMed: 17064730] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND MAGNESIUM IONS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842580 Genomic DNA. Translation: CAB08916.1.
AE000516 Genomic DNA. Translation: AAK46877.1.

PIR

B70550.

RefSeq

NP_217014.1. NC_000962.2.
NP_337063.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U5H	X-ray	1.65	A	1-273	[»]
1U5V	X-ray	1.85	A	1-273	[»]
1Z6K	X-ray	2.30	A	1-273	[»]

ProteinModelPortal

O06162.

SMR

O06162. Positions 1-223.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000003910; EBMYCP00000003910; EBMYCG00000003908.
EBMYCT00000069192; EBMYCP00000067251; EBMYCG00000069187.

GeneID

887466.
925758.

GenomeReviews

Gene locus MT2573 in contig AE000516_GR.
Gene locus Rv2498c in contig AL123456_GR.

KEGG

mtc:MT2573.
mtu:Rv2498c.

PATRIC

18127414. VBIMycTub22151_2812.

TIGR

MT2573.

Organism-specific databases

TubercuList

Rv2498c.

Phylogenomic databases

GeneTree

EBGT00050000015626.

HOGENOM

HBG676713.

OMA

AWLFCPA.

PhylomeDB

O06162.

ProtClustDB

CLSK791885.

Family and domain databases

InterPro

IPR005000. Aldehyde-lyase_domain.
IPR011206. Citrate_lyase_beta.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]

Gene3D

G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

KO

K01644.

PANTHER

PTHR11105. PTHR11105. 1 hit.

Pfam

PF03328. HpcH_HpaI. 1 hit.
[Graphical view]

PIRSF

PIRSF015582. Cit_lyase_B. 1 hit.

SUPFAM

SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

CITEL_MYCTU

Accession

Primary (citable) accession number: O06162
Secondary accession number(s): Q7D713

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program