Reviewed, UniProtKB/Swiss-Prot P45303 (ODO1_HAEIN)

Names and origin

Protein names

Recommended name:
    2-oxoglutarate dehydrogenase E1 component
    EC=1.2.4.2
Alternative name(s):
    Alpha-ketoglutarate dehydrogenase

Gene names

Name:	sucA
Ordered Locus Names:	HI1662

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	935 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: InterPro thiamin pyrophosphate binding 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 – 935	935	2-oxoglutarate dehydrogenase E1 component		PRO_0000162194

Sequences

	Sequence		Length	Mass (Da)
	P45303-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 33607F3C3AFDDC78	FASTA	935	106,806
	10 20 30 40 50 60 MQQNKAFDDW LASTALGGAN QSYIEELYES YLSDPQSVEE SWRKTFDSLP KTTALEQPHT 70 80 90 100 110 120 PVRDYFRRLA RENHNEAVTV IDPAAGAKLV KVLQFINAYR FRGHLEANLD PLNYYRWKVS 130 140 150 160 170 180 FVPELDYRHH GFTEQDLNET FNINHYVYKR DTIKLGELAQ MLKETYCGSI GLEFMHVQDM 190 200 210 220 230 240 EQKMWLQSKM ESLLDKPLFT SEERVNFLRE LTAADGLERY LGAKFPGAKR FSLEGSDAFI 250 260 270 280 290 300 PLMKEIIRHS SRQGVNDVVM GMAHRGRLNM LVNVLGKKPE NLFDEFAGKH SSERTGDVKY 310 320 330 340 350 360 HQGFSSDFAV DDKRVHLTLA FNPSHLEIVS PVVIGSVRSR QTRMNDTEHS KVLAITVHGD 370 380 390 400 410 420 SAVAGQGVVQ ETLNMSNTRG YSVGGTIRIV INNQIGFTTS NPNDTRSTEY CTDIAKMIQA 430 440 450 460 470 480 PIIHVNGDDP EAVAFAARMA VEYRNLFKRD IFIDLISYRR HGHNEADEPL ATQPMMYSII 490 500 510 520 530 540 KKHPTPRKVY ADRLVSEGVM TEEQVTEMAN DYRDALDNGD RVVSEWREMD TAKMDWLQYL 550 560 570 580 590 600 NYDWTAPYES KFSQERFLTL AKRVCEYPES LRAHPRVEKI YNDRKAMYQG EKLLDWGMAE 610 620 630 640 650 660 TMAYATLLDE GVNVRLSGED AGRGTFFHRH AVVHNQNDGT GYVPLTHLHA NQGRFEVWDS 670 680 690 700 710 720 VLSEESVLAF EYGYATTDPK TLTIWEAQFG DFANGAQIVI DQFISSGEQK WGRMCGLVML 730 740 750 760 770 780 LPHGYEGQGP EHSSARLERY LQLCAEQNMQ VCVPSTPAQV YHMLRRQSLR KMRRPLIAIS 790 800 810 820 830 840 PKSLLRHPLA VSSLDELING TFQTVIGEID ELDPKDVKRV VMCSGKVYYD LLEQRRANNQ 850 860 870 880 890 900 KDVAIIRIEQ LYPFPHEDVK KALEPYAHVT DYVWCQEEPL NQGAWYCSKH NFESAIPESV 910 920 930 KLKYAGRPAS ASPAVGYMSL HTKQQKQLVE DALSF

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
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC23308.1. Different initiation.
PIR	E64135.
RefSeq	NP_439804.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	950496.
GenomeReviews	Gene locus HI1662 in contig L42023_GR.
KEGG	hin:HI1662.
NMPDR	fig|71421.1.peg.1576.
TIGR	HI1662.
Phylogenomic databases
HOGENOM	P45303.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1662-MON.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DHase_E1. IPR001017. DHase_E1. IPR005475. Transketo_Cen_R. [Graphical view]
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODO1_HAEIN

Accession

Primary (citable) accession number: P45303

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)