ID   A0A1G6TIB0_9ACTN        Unreviewed;       655 AA.
AC   A0A1G6TIB0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:SDD28604.1};
GN   ORFNames=SAMN05421872_10783 {ECO:0000313|EMBL:SDD28604.1};
OS   Nocardioides lianchengensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1045774 {ECO:0000313|EMBL:SDD28604.1, ECO:0000313|Proteomes:UP000199034};
RN   [1] {ECO:0000313|EMBL:SDD28604.1, ECO:0000313|Proteomes:UP000199034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6858 {ECO:0000313|EMBL:SDD28604.1,
RC   ECO:0000313|Proteomes:UP000199034};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMZM01000007; SDD28604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6TIB0; -.
DR   STRING; 1045774.SAMN05421872_10783; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000199034; Unassembled WGS sequence.
DR   GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03710; OAFO_sf; 1.
DR   PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199034}.
FT   DOMAIN          24..216
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          265..479
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          531..601
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   655 AA;  69319 MW;  5B698A4D16D92EB0 CRC64;
     MTGQQSKQVK QLDRVIIRFA GDSGDGMQLT GDRFTSESAV FGNDLMTLPN FPAEIRAPQG
     TIPGVSSFQV HFADHDILTA GDAPDVLVAM NPAALKANLA DLPKGAIIIV DTHDFTTRNL
     TKAGYDANPL DALGDAGSAL GEFAVHAVDL TGMTVEAVKE FGLSRKDAAR AKNMFALGLL
     SWMYGRPTES TTAFLTKRFA RVPDIRDANI TAFKAGWNFG ETTESFAVSY EIKPAPQQPG
     TYRNISGNLA LAYGLVAAGV QSGLPVFLGT YPITPASDIL HELSKHKSFG VTTFQAEDEI
     AGVGAAIGAS FAGSLGVTST SGPGVALKSE AIGLAVMTEL PLLVVNVQRG GPSTGLPTKT
     EQADLLQAMF GRNGEAPVPI VAPQSPGDCF AAAVEAARIA VTYRTPVFLL SDGYLANGSE
     PWAIPDVADL PVIEPRFATE HNHTKTAPDG TVSTEFWPYL RDEETLARPW AVPGTAGLEN
     RIGGLEKGEG HGNISYDPAN HDLMVRTRQA KIDRIAESIP PLQVDDPSGA AKVCVLGWGS
     TYGPIGAAAR RVRKAGFNVA QVHLRHLNPF PKDLGEILRR YDKVLVPEMN LGQLSMLIRA
     RYLVDAVGYN QVNGMPIKAA QLAEAVGALV ADAEGTPVDL TADLTPATTA QEVSE
//