ID A0A080M9G1_9PROT Unreviewed; 946 AA.
AC A0A080M9G1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=sucA {ECO:0000313|EMBL:KFB77947.1};
GN ORFNames=AW06_000739 {ECO:0000313|EMBL:KFB77947.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77947.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB77947.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFB77947.1}.
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DR EMBL; JDST02000013; KFB77947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M9G1; -.
DR STRING; 1453999.AW06_000739; -.
DR Proteomes; UP000021315; Unassembled WGS sequence.
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:KFB77947.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 592..789
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 946 AA; 106340 MW; 9BEE9845F2228D2F CRC64;
MMNQLFGNSL LFGGNAPFVE ELYENYLDNP GSVSDQWREY FDKLAQLPGY VARDVPHLPV
INAFAELARK GGYRAAAVTP VDDRKQVSVL QMITSYRFIG DRWANLDPLK RTPRPEVPQL
DPAYYGLSDA DLNTVFNAGS FKGTPDHATF GQIYDALKAT YCGSIGVEYM YISTVAEKRW
IQDRLERIHS KPNYTAEQRR RMLERLTAAE TLERYLHTRY VGQKRFSLEG GESTIVAMDE
LIRVAGAGGV DEIVVGMAHR GRLNVLVNTL GKAPSMLFDE FEGKKAQILT AGDVKYHMGY
SSDVSTPGGP CHLTLAFNPS HLEIVNPVVV GSVYSRQRRR GENGKDKVLS VLIHGDAAVA
GQGVNQEMLN FAQTRGYGVG GTVHIVINNQ IGFTTSDPRD YRSSLYCTDI FKMAEAPIFH
VNGDDPEAVA LVTSLAVEFR KTFKKDVVVD IVCYRKLGHN EQDEPMVTQP LMYKKIQQHP
GTRKLYADKL VAEGVLHAEG PNEIIADYRA HLDRGELLYN PVLAGYKHPM TIDWTPFVSP
QYIENCDTKV PVGELQRLSE RLTTIPPNFT LHSRVQKIIE DRRQMGEGKL PVDWGMAENL
AYASLLVSGY GVRISGEDVG RSTFFHRHAA LHDQNREHWD HGTYYPLANL QERQGGFQCF
DSVLSEEAVL AFEYGYSTAN PHELVVWEAQ FGDFANGAQV VIDQFIAAGE AKWGRASGLV
LLLPHGYEGQ GPEHSSARIE RYMQLCAEMN MEVCQPSTPA QVFHMLRRQA LRSQRKPLIV
FSPKSLLRHK DATSTLEELS DGEFQRVIGE VEPIIAKKVT RVIFCSGKIY YELVAARHER
KVSHVAIARL EQLYPFPQES FQEELAKYPK ATEVVWCQDE PRNQGAWYWI ASRQHLSRSL
SDKQHLLLVS RPASASPAVG YQSKHNAQQK ALIDSAFGEI EYYKLP
//
