ID Q0C5F1_HYPNA Unreviewed; 1002 AA.
AC Q0C5F1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
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:ABI78622.1};
GN OrderedLocusNames=HNE_0312 {ECO:0000313|EMBL:ABI78622.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI78622.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI78622.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI78622.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI78622.1; -; Genomic_DNA.
DR RefSeq; WP_011645342.1; NC_008358.1.
DR AlphaFoldDB; Q0C5F1; -.
DR STRING; 228405.HNE_0312; -.
DR KEGG; hne:HNE_0312; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR Proteomes; UP000001959; 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:ABI78622.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001959};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 637..830
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 111591 MW; AC5C56744623218E CRC64;
MADDGSPVNG PRSTGNAAML DTAFLYGASA QWLEQMQAAY AKNPNSVPES WRAFFAELGD
EPASAKQNAD GASWKRKDWP RPASSEQIAA FDGDWALLEP KIEKKIKSGA PGIAAEDLGR
AVTDSIRALM MIRAYRMRGH LAAQLDPLGL SGFGDQPELD PASYGFGPAD MDRSIYIDGY
LGLDRATPAQ MLDILRRTYC STLGIEFMHI SDPEEKSWLQ ERIEGPDKGV AFTREGKIAI
LRKLIEAEAF ERFLHKRYPG TKRFGLDGGE AAVPALEQII KRGGALGVNE IIVGMPHRGR
LNMLAAVMGK GYEKIFHEFQ GGSTQGAGEF GSGDVKYHLG ASSDREFDGN VVHLTMNPNP
SHLEAVNPVV LGRTRAKQFM ESRETGKLDR SHKMPLLLHG DAAFAGQGVV AECFALSGLQ
GYRTGGTIHF IVNNQIGFTT SPMYSRSSPY PSDVALMVQA PIFHVNGDDP EAVVYAAKVA
TEYRQKFAKD VVIDMFCYRR FGHNEGDDPT MTQPVMYRVI KERPSTREIY AQRLVAEGLL
TAAEVETQVK EFEDFLDRAF DAGKTLKTNK ADWLEGQWSG FGLPLDDDRR GKTGVSKTRL
KELGDAITAI PENVDAHKTV ERVLARRRES YETGKEIDWG GAEHLAFASL VDEGFPVRLS
GQDSGRGTFV QRHSHIVDQT TGDRITLLNQ IREGQAPYEV IDSLLSEEAV LGYEYGYSLT
DPNTLTCWEA QFGDFANGAQ VYYDQFISSA ERKWLRMSGL VMLLPHGYEG QGPEHSSARL
ERFLQMCAED NMQVCNLTTP ANYFHALRRQ IHREFRKPLV IMTPKSLLRH KLATSTLDDM
NTKSTFHRIL WDDAETPGRE GKVKLAKDNK VRRVVLCSGK VYYDLFEARE ASGQDDVYLL
RVEQFYPVPR KSLITELKRF PQAELVWCQE EPRNMGGWTF IRDEIEWCAA QAGYKQPRPK
YAGRPPSAAT ATGLLSKHQA EQANLLKTAL SPDPVDDRIV SP
//
