ID   F8KZ57_PARAV            Unreviewed;       915 AA.
AC   F8KZ57;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
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:CCB86180.1};
GN   OrderedLocusNames=PUV_12300 {ECO:0000313|EMBL:CCB86180.1};
OS   Parachlamydia acanthamoebae (strain UV7).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Parachlamydia.
OX   NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB86180.1, ECO:0000313|Proteomes:UP000000495};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UV7;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA   Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA   Myers G.S.A., Horn M.;
RT   "Unity in variety -- the pan-genome of the Chlamydiae.";
RL   Mol. Biol. Evol. 0:0-0(2011).
RN   [2] {ECO:0000313|EMBL:CCB86180.1, ECO:0000313|Proteomes:UP000000495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX   PubMed=21690563; DOI=10.1093/molbev/msr161;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA   Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA   Myers G.S., Horn M.;
RT   "Unity in variety--the pan-genome of the Chlamydiae.";
RL   Mol. Biol. Evol. 28:3253-3270(2011).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FR872580; CCB86180.1; -; Genomic_DNA.
DR   RefSeq; WP_013924836.1; NC_015702.1.
DR   AlphaFoldDB; F8KZ57; -.
DR   STRING; 765952.PUV_12300; -.
DR   KEGG; puv:PUV_12300; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_0; -.
DR   Proteomes; UP000000495; 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:CCB86180.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000495};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          573..766
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   915 AA;  104342 MW;  026AD3A58CDD8FA4 CRC64;
     MTSYNALIQS GFANLALIDE MYAKFQADPH SVDSSWRHLF EEAKPGATQT FPSDRRGIDQ
     MLIDQVAAGG VRIYHLIEAY RTYGHYMAKV NPIATAPIEE PWQLKLETLG FTPEELSHRF
     PTCGLLNEAS ATLQELINCL REIYCENIGI EYMGLENPDM EKWLQNHIEP TRFKIELTFE
     QKRLILQHLN KSELFELFLH TKYTGQKRFS LEGGETLIPI LDAIIEKGSQ EGVEEFVLGM
     AHRGRLNVLS NILDKSYADI FSEFDEGYIP DSFEGSGDVK YHKGFSSNVQ TATGHKVRVE
     MPPNPSHLES VDAVVEGEVY ARQILASDHE TKKKVLPILV HGDAAISGQG VCYETMQMYD
     LPGYSTGGTI HVVINNQIGF TTLPRDSRST HYCTDIARTF RAPVFHVNAE DPEACVYATL
     LAVQLRQKYR CDVFIDLNCY RKFGHNETDE PAYTQPYQYQ LIRQKKPIRE LYRDNLIHQG
     ILEKQMAESL EHEFKESLQK ALQETKIPTE KVKKVKSEDA DELFVTYPTG VPQDTLVEVT
     EKLSTIPPDF HIHRKLENLI QDRRQMGIGQ KSVDWGMAET LAYGTLLWDG VSVRISGQDV
     CRGTFSHRHA MWVDQQTDQP YFPLQHLKEK QGRFNIYNSP LSEYAVLAFE YGYSIGNPKA
     LVIWEAQFGD FANGAQIVID QYISAAEEKW GQKVGLVMLL PHGYEGQGPE HSSARIERFL
     TLAGDCNMQI VNPTTPAQFF HLLRRQTMLA SLKPLVVFTP KGLLRHPAAQ NPIQDFVNGS
     FQDIYDDPRA SKKVKTLLFC SGRFYYDLDE ERKKQGVEDM VIVRIEQLYP LNVKKLLEII
     KKYEGFSRCA WVQEEPRNMG AWNFIRPKLR EILPSTLELE YIGRACKASP AVGSYALHKQ
     EHAEIIQAIF GKKAK
//