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Database: UniProt
Entry: V8CG66_9HELI
LinkDB: V8CG66_9HELI
Original site: V8CG66_9HELI 
ID   V8CG66_9HELI            Unreviewed;       374 AA.
AC   V8CG66;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=2-oxoglutarate synthase subunit alpha {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF2087_01813 {ECO:0000313|EMBL:ETD25975.1};
OS   Helicobacter canis NCTC 12740.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1357399 {ECO:0000313|EMBL:ETD25975.1, ECO:0000313|Proteomes:UP000018688};
RN   [1] {ECO:0000313|EMBL:ETD25975.1, ECO:0000313|Proteomes:UP000018688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 12740 {ECO:0000313|EMBL:ETD25975.1,
RC   ECO:0000313|Proteomes:UP000018688};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Fox J.G., Shen Z., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Helicobacter canis NCTC 12740.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:ETD25975.1}.
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DR   EMBL; AZJJ01000007; ETD25975.1; -; Genomic_DNA.
DR   RefSeq; WP_023930872.1; NZ_KI669458.1.
DR   AlphaFoldDB; V8CG66; -.
DR   STRING; 1357399.HMPREF2087_01813; -.
DR   PATRIC; fig|1357399.3.peg.1902; -.
DR   eggNOG; COG0674; Bacteria.
DR   HOGENOM; CLU_017038_0_1_7; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000018688; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR32154:SF14; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORA; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018688}.
FT   DOMAIN          14..243
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          275..367
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   374 AA;  41264 MW;  7082760C47929D77 CRC64;
     MREVISGGNE LVAKAAIDAG CRFYGGYPIT PSSDIMHEMS VLLPKHNGHF IQMEDEISGI
     CAALGAAMSG VKSMTGSSGP GISLKVEQIG LGFMAEVPLV IADVMRSGPS TGMPTRVAQG
     DVGFLKHPTH GDFKSVAIAP GNLEESYTQT IRAFNLAEEL MTPVFLLMDE TIGHMYGKTY
     IPDIEEVQKS VINRRTFTGD PKSYQPYDVK PDEGAILNPF FQGYRYHITG LHHGPLGFPT
     EDAKMGQALI DRLFNKIESK ESYICQNEEL DLEGAEIAII AYGSTALSVK EAMIELKKMG
     KKVGLFRPIT LWPSPKTRLK QLGETYKKIL VIELNKGQYL EEIERVLERK VEFMGQANGR
     SISPTQIIDR IKEM
//
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