ID B4RCH5_PHEZH Unreviewed; 982 AA.
AC B4RCH5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 Name=sucA {ECO:0000313|EMBL:ACG76574.1};
GN OrderedLocusNames=PHZ_c0160 {ECO:0000313|EMBL:ACG76574.1};
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG76574.1, ECO:0000313|Proteomes:UP000001868};
RN [1] {ECO:0000313|EMBL:ACG76574.1, ECO:0000313|Proteomes:UP000001868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG76574.1,
RC ECO:0000313|Proteomes:UP000001868};
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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}.
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DR EMBL; CP000747; ACG76574.1; -; Genomic_DNA.
DR RefSeq; WP_012520722.1; NC_011144.1.
DR AlphaFoldDB; B4RCH5; -.
DR STRING; 450851.PHZ_c0160; -.
DR KEGG; pzu:PHZ_c0160; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000001868; 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 Reference proteome {ECO:0000313|Proteomes:UP000001868};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 628..821
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 982 AA; 108943 MW; EBEDEC9E4385548F CRC64;
MADDAGLINE VLAETSFLYG GNAAFVEDLY AKWAANPESV EPSWRAFFAS LADRADEVKA
AAQRPAWTRP SAPQPRPEWL SAIDGLWPAV EAKLGQKVAE RKPAATQDEV RAATLDSLRA
IMMIRAYRMR GHLKANLDPL EIATTPGDAS ELDPATYGFA EADFDRPIFL DYVLGLETAT
LREILEILRR TYCGNVGVQY MHISDPKEKA WLQERIEGRD KEIAFTKEGK VAILKKLIEA
EGFERFLHRR FPGTKRFGLD GGEAMVPALE QIIKRGGAMG VKDIVVGMPH RGRLNVLAAV
MGKPYHIIFH EFQGGSSVPS DVEGSGDVKY HLGASSDREF DGNSVHLSLT ANPSHLEIVN
PVVIGKARAK QAFTLRDNPD AGRSHVLPLL LHGDAAFAGQ GVVAECFALS GLKGYGVGGT
MHFVVNNQIG FTTSPKNSRS SPYPSDVALM VEAPIFHVNG DDPEAVVFAA KVATEYRQLF
GKDVVVDMFC YRRFGHNEGD DPTMTQPLMY AKIKGHPSVK DLYAQRLVAE GVVSQAEADG
WTAEFEAFLD AEFDSGKVYK ANKADWLDGK WSGRKPSGEE KPTTGVPKQK LLDLGRKMTS
IPERITAHKT VERVISARRD AIEKGEGIDW ATAEHLAFAT LLDQGYPVRL SGQDSVRGTF
SQRHSGLIDQ KTEEVYFPLR NLGPSQAHFE VLDSALSEEA VLGFEYGFSL TDPDTLVMWE
AQFGDFANGA QVVVDQFISS GERKWLRMSG LTLLLPHGYE GQGPEHSSAR LERYLQLCAE
ENMQVVHPTT PANYFHVLRR QMVREFRKPL IVMTPKSLLR HKRAVSNLVD MAEGSSFHRV
LVDGAEAGCD VGGVTLKPDD KITRVILCSG KVYFDLVEHR AKTGRDDIYL LRLEQFYPWP
MKSVTNELKR FKNAELIWCQ EEPKNMGGWT FVDPWLELTL ERMNVKAKRA RYVGRPASAS
TAAGLMSRHL KELEAFLTEA FA
//
