O50463 (KGD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-oxoglutarate decarboxylase
EC=4.1.1.71

Alternative name(s):
2-oxoglutarate carboxy-lyase
Alpha-ketoglutarate decarboxylase

Gene names

Name:	kgd
Ordered Locus Names:	Rv1248c, MT1286

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1231 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes an oxidative decarboxylation from five-carbon 2-oxoglutarate (alpha-ketoglutarate) to four-carbon succinate semialdehyde. Ref.3 Ref.4
Catalytic activity	2-oxoglutarate = succinate semialdehyde + CO2. Ref.4
Cofactor	Magnesium. Ref.4 Thiamine pyrophosphate. Ref.4
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Kgd subfamily.
Caution	Was originally (Ref.1 and Ref.2) annotated as sucA because of sequence similarity, however, this protein was shown (Ref.3) not to be able to serve as the E1 component of 2-oxoglutarate dehydrogenase (KDH).
Biophysicochemical properties	Kinetic parameters: KM=0.48 mM for alpha-ketoglutarate Ref.4 KM=0.196 mM for magnesium ions KM=0.019 mM for thiamine pyrophosphate
Sequence caution	The sequence CAA15904.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Domain	Coiled coil
Ligand	Magnesium Thiamine pyrophosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE tricarboxylic acid cycle Inferred from direct assay Ref.4. Source: MTBBASE
Cellular component	plasma membrane Inferred from direct assay. Source: MTBBASE pyruvate dehydrogenase complex Inferred from direct assay Ref.3. Source: MTBBASE
Molecular function	2-oxoglutarate decarboxylase activity Inferred from direct assay Ref.4. Source: MTBBASE electron carrier activity Inferred from direct assay Ref.3. Source: MTBBASE magnesium ion binding Inferred from direct assay Ref.4. Source: MTBBASE oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: MTBBASE thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring acyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1231	1231	2-oxoglutarate decarboxylase		PRO_0000310722
Regions
	Coiled coil	787 – 817	31	Potential
	Compositional bias	61 – 113	53	Ala-rich

Sequences

	Sequence		Length	Mass (Da)
	O50463 [UniParc]. Last modified November 13, 2007. Version 4. Checksum: 96C255612BA12889	FASTA	1,231	135,902
	10 20 30 40 50 60 MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTSQPAA EPTRVTSPLV 70 80 90 100 110 120 AERAAAAAPQ APPKPADTAA AGNGVVAALA AKTAVPPPAE GDEVAVLRGA AAAVVKNMSA 130 140 150 160 170 180 SLEVPTATSV RAVPAKLLID NRIVINNQLK RTRGGKISFT HLLGYALVQA VKKFPNMNRH 190 200 210 220 230 240 YTEVDGKPTA VTPAHTNLGL AIDLQGKDGK RSLVVAGIKR CETMRFAQFV TAYEDIVRRA 250 260 270 280 290 300 RDGKLTTEDF AGVTISLTNP GTIGTVHSVP RLMPGQGAII GVGAMEYPAE FQGASEERIA 310 320 330 340 350 360 ELGIGKLITL TSTYDHRIIQ GAESGDFLRT IHELLLSDGF WDEVFRELSI PYLPVRWSTD 370 380 390 400 410 420 NPDSIVDKNA RVMNLIAAYR NRGHLMADTD PLRLDKARFR SHPDLEVLTH GLTLWDLDRV 430 440 450 460 470 480 FKVDGFAGAQ YKKLRDVLGL LRDAYCRHIG VEYAHILDPE QKEWLEQRVE TKHVKPTVAQ 490 500 510 520 530 540 QKYILSKLNA AEAFETFLQT KYVGQKRFSL EGAESVIPMM DAAIDQCAEH GLDEVVIGMP 550 560 570 580 590 600 HRGRLNVLAN IVGKPYSQIF TEFEGNLNPS QAHGSGDVKY HLGATGLYLQ MFGDNDIQVS 610 620 630 640 650 660 LTANPSHLEA VDPVLEGLVR AKQDLLDHGS IDSDGQRAFS VVPLMLHGDA AFAGQGVVAE 670 680 690 700 710 720 TLNLANLPGY RVGGTIHIIV NNQIGFTTAP EYSRSSEYCT DVAKMIGAPI FHVNGDDPEA 730 740 750 760 770 780 CVWVARLAVD FRQRFKKDVV IDMLCYRRRG HNEGDDPSMT NPYVYDVVDT KRGARKSYTE 790 800 810 820 830 840 ALIGRGDISM KEAEDALRDY QGQLERVFNE VRELEKHGVQ PSESVESDQM IPAGLATAVD 850 860 870 880 890 900 KSLLARIGDA FLALPNGFTA HPRVQPVLEK RREMAYEGKI DWAFGELLAL GSLVAEGKLV 910 920 930 940 950 960 RLSGQDSRRG TFSQRHSVLI DRHTGEEFTP LQLLATNSDG SPTGGKFLVY DSPLSEYAAV 970 980 990 1000 1010 1020 GFEYGYTVGN PDAVVLWEAQ FGDFVNGAQS IIDEFISSGE AKWGQLSNVV LLLPHGHEGQ 1030 1040 1050 1060 1070 1080 GPDHTSARIE RFLQLWAEGS MTIAMPSTPS NYFHLLRRHA LDGIQRPLIV FTPKSMLRHK 1090 1100 1110 1120 1130 1140 AAVSEIKDFT EIKFRSVLEE PTYEDGIGDR NKVSRILLTS GKLYYELAAR KAKDNRNDLA 1150 1160 1170 1180 1190 1200 IVRLEQLAPL PRRRLRETLD RYENVKEFFW VQEEPANQGA WPRFGLELPE LLPDKLAGIK 1210 1220 1230 RISRRAMSAP SSGSSKVHAV EQQEILDEAF G

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]	"Mycobacterium tuberculosis appears to lack alpha-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes." Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C. Mol. Microbiol. 57:859-868(2005) [PubMed: 16045627] [Abstract] Cited for: LACK OF FUNCTION AS A 2-OXOGLUTARATE DEHYDROGENASE. Strain: ATCC 25618 / H37Rv.
[4]	"Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: identification of alpha-ketoglutarate decarboxylase." Tian J., Bryk R., Itoh M., Suematsu M., Nathan C. Proc. Natl. Acad. Sci. U.S.A. 102:10670-10675(2005) [PubMed: 16027371] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTORS, ROLE IN TRICARBOXYLIC ACID CYCLE, KINETIC PARAMETERS. Strain: ATCC 25618 / H37Rv.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842576 Genomic DNA. Translation: CAA15904.1. Different initiation. AE000516 Genomic DNA. Translation: AAK45544.1.
PIR	G70953.
RefSeq	NP_335730.1. NC_002755.2.
3D structure databases
ProteinModelPortal	O50463.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000002347; EBMYCP00000002347; EBMYCG00000002345. EBMYCT00000069310; EBMYCP00000067369; EBMYCG00000069305.
GeneID	924785.
GenomeReviews	Gene locus MT1286 in contig AE000516_GR. Gene locus Rv1248c in contig AL123456_GR.
KEGG	mtc:MT1286. mtu:Rv1248c.
PATRIC	18124592. VBIMycTub22151_1415.
TIGR	MT1286.
Organism-specific databases
TubercuList	Rv1248c.
Phylogenomic databases
GeneTree	EBGT00050000014858.
HOGENOM	HBG289950.
OMA	EGDEPAF.
PhylomeDB	O50463.
ProtClustDB	PRK12270.
Family and domain databases
InterPro	IPR001078. 2-oxoacid_DH_actylTfrase. IPR011603. 2oxoglutarate_DH_E1. IPR023213. CAT-like_dom. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
Gene3D	G3DSA:3.30.559.10. CAT-like_dom. 1 hit.
KO	K01616.
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KGD_MYCTU

Accession

Primary (citable) accession number: O50463
Secondary accession number(s): Q7D8I9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 77 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program