B9EC10 (B9EC10_MACCJ) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
2-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169
EC=1.2.4.2 HAMAP-Rule MF_01169

Alternative name(s):
Alpha-ketoglutarate dehydrogenase HAMAP-Rule MF_01169

Gene names

Name:	odhA HAMAP-Rule MF_01169
Ordered Locus Names:	MCCL_1064 EMBL BAH17771.1

Organism

Macrococcus caseolyticus (strain JCSC5402) [Complete proteome] [HAMAP] EMBL BAH17771.1

Taxonomic identifier

458233 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Macrococcus › Macrococcus caseolyticus

Protein attributes

Sequence length	925 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. HAMAP-Rule MF_01169 SAAS SAAS023784
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. HAMAP-Rule MF_01169 SAAS SAAS023784
Cofactor	Thiamine pyrophosphate By similarity. HAMAP-Rule MF_01169 SAAS SAAS023784
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_01169 SAAS SAAS023784
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family. HAMAP-Rule MF_01169

Ontologies

Keywords
Biological process	Glycolysis SAAS SAAS023784 HAMAP-Rule MF_01169
Ligand	Thiamine pyrophosphate SAAS SAAS023784 HAMAP-Rule MF_01169
Molecular function	Oxidoreductase SAAS SAAS023784 HAMAP-Rule MF_01169
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Molecular_function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: HAMAP thiamine pyrophosphate binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B9EC10 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: CF4BA9E54754A667	FASTA	925	104,156
	10 20 30 40 50 60 MTKGKNLEEA PPRFGTNLGI LLEMFDQYQN DPSSVSDELQ ELFSNIQRGS TGHSGMGSTD 70 80 90 100 110 120 ADIVKRLMRL IDNIRQYGHL KADIYPLYKP KRDQHIKLSI EDFGLSEEVL KQLPASLVSE 130 140 150 160 170 180 HYGERLNNAF EAITEMQQTY QGPIAYEVSH INNSEEREWL KTTIESKVKR DFSKEEKVEL 190 200 210 220 230 240 LKSVARVEGF EKYIHKNFVG AKRFSIEGVD ALVPMLENVI KFAGENNIQD IEIGMAHRGR 250 260 270 280 290 300 LNVLTHILEK PYEMMLSEFM HTDPMKFLPE DGSLVVKKGW TGDVKYHLGG IKTTTRFGKT 310 320 330 340 350 360 QTISLANNPS HLEIVAPVVL GKTRAVQEVT DGVNEPKQDF NKALAVLIHG DAAFPGQGIN 370 380 390 400 410 420 FESMNLSNLK GYSVGGSLHI ITNNRVGFTT ESYDSRSTTY ATDVAKGYDL PIIHVNADDL 430 440 450 460 470 480 EACIEAIEVA MAYRQKFNKD FVIDLVGYRR YGHNEMDEPT VTNPMLYKEV KGHPSIEILY 490 500 510 520 530 540 GKSLVEASVI TEDEMNAIFE DVASRLRSAH DAIDKSSVNN DSEMKMPEAV EAGYEKIDTG 550 560 570 580 590 600 VALEKLKQLN DDMLSIPEQF SVFNKLQKIL ERRNDPFTKD GLVDWGHAEL LAYGTIIQDG 610 620 630 640 650 660 NPVRHTGQDA ERGTFAHRHA VLHDVKNGDK YIPLQHIEGA QSSFDIHNSP LSEAAVVGFE 670 680 690 700 710 720 YGYNLQNNKA LTVWEAQYGD FANMAQMIFD NFISSAEAKW GEKSGLTLLL PHAYEGQGPE 730 740 750 760 770 780 HSSARLERFL QLAAEHNWTV ANLSSTANYF HLLRRQAQYL GTDRMRPLVI MSPKSLLRNS 790 800 810 820 830 840 FVSDTIEKFT EGSFKAIISS EYKKTKVKKL LIASGKVAVD LMTELTKNPN DEVHVIRLEQ 850 860 870 880 890 900 IYPFPEQDIK AIIDDLKGLT EIGFVQEEPK NQGSWHYIYP LLNNIKPAKV KLSYYGRPYR 910 920 AAPAEGDNEI HKIVQSKLIS EALNI

References

[1]

"Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, [corrected] reflecting the ancestral genome of the human-pathogenic staphylococci." Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K. J. Bacteriol. 191:1180-1190(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC5402 EMBL BAH17771.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009484 Genomic DNA. Translation: BAH17771.1.
RefSeq	YP_002560467.1. NC_011999.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	458233.MCCL_1064.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAH17771; BAH17771; MCCL_1064.
GeneID	7390741.
KEGG	mcl:MCCL_1064.
PATRIC	22424493. VBIMacCas48391_1189.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0567.
HOGENOM	HOG000259588.
KO	K00164.
OMA	QEVQKYP.
ProtClustDB	PRK09404.
Enzyme and pathway databases
BioCyc	MCAS458233:GI03-801-MONOMER.
Family and domain databases
HAMAP	MF_01169. SucA_OdhA.
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR023784. 2oxoglutarate_DH_E1_bac. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. PTHR23152. 1 hit.
Pfam	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

B9EC10_MACCJ

Accession

Primary (citable) accession number: B9EC10

Entry history

Integrated into UniProtKB/TrEMBL:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)