ID Q1QQR5_NITHX Unreviewed; 989 AA.
AC Q1QQR5;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN OrderedLocusNames=Nham_0542 {ECO:0000313|EMBL:ABE61432.1};
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE61432.1, ECO:0000313|Proteomes:UP000001953};
RN [1] {ECO:0000313|EMBL:ABE61432.1, ECO:0000313|Proteomes:UP000001953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14
RC {ECO:0000313|Proteomes:UP000001953};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000319; ABE61432.1; -; Genomic_DNA.
DR RefSeq; WP_011509136.1; NC_007964.1.
DR AlphaFoldDB; Q1QQR5; -.
DR STRING; 323097.Nham_0542; -.
DR KEGG; nha:Nham_0542; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000001953; Chromosome.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABE61432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001953};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 636..829
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 989 AA; 111125 MW; 3BCFCBB5272BCE55 CRC64;
MSRQNANAAF ALSSFLQGAN ATYIDGLYAR YEKDPGSVDA EWQEFFKSLK DAPDDVRKNA
KGPSWEKANW PLAPQDDLIS ALDGNWTQIE KAVGAKLQAK AQGEAQARDS ALAGVDVNQA
TRDSVRALML IRAYRMRGHF HARLDPLGLE PARDHEELDP RAYGFTDADM DRKIFLDHVL
GLEYGTLREI VAICERTYCQ TLGVEFMHIS NGAQKGWIQE RIEGPDKEIS FTPEGRRAIL
KKLVEAEGFE KFCDVKFTGT KRFGLDGGES LIPALEQIIK RGGNLGVKEI VIGMPHRGRL
NVLTQVMGKP HRALFHEFKG GSANPDVVEG SGDVKYHLGA SSDREFDNNR IHLSLTANPS
HLEIVDPVVL GKVRAKQDQH GDPPDQRDSV LPLLMHGDAA FAGQGVVAEC FALSDLKGYR
TGGSIHFIVN NQIGFTTYPR YSRSSPYPSD LAKMIDAPIF HVNGDDPEAV VFAAKVAIEF
RQKFHKPVVI DMFCYRRHGH NEGDEPSFTN PMMYKKIAAH PSTLELYAKR LSTEGVITDG
EIEKLKADWR ARLDAEFEAG AGYKPNKADW LDGKWAGFKL ADQDEEPRRG VTGVDIATLK
QIGRSITRVP DGFRVHRTVQ RFLDNRAKAI DRGVGIDWAT AEALAFCTLV LEGHNVRLSG
QDSERGTFSQ RHSVLFDQED ESRYTPFNHL GKDQGRYEVI NSLLSEEAVL GFEYGYSLAE
PNTLTLWEAQ FGDFANGAQV LFDQFISSGE RKWLRMSGLV CMLPHGYEGQ GPEHSSARLE
RFLQMCAEDN MQVVNISTPA NHFHALRRQL KRQIRKPLIM MTPKSLLRHK RAVSRLDELG
ADTAFHRILY DDATILPDQK IRLVEDEKIR RVVLCSGKVY YDLYEERAKR DIADVYLLRI
EQLYPVPLKA LVQVLGRFNK AEIVWCQEEP RNMGAWHFIE PYLEWVLNQI DAPNKRPRYA
GRAAAAATAT GLMSKHLAQL KALLDEALD
//
