ID A0A138AQ34_9ACTN Unreviewed; 1193 AA.
AC A0A138AQ34;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:KXP12554.1};
GN ORFNames=AXK60_04890 {ECO:0000313|EMBL:KXP12554.1};
OS Tsukamurella pseudospumae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=239498 {ECO:0000313|EMBL:KXP12554.1, ECO:0000313|Proteomes:UP000070258};
RN [1] {ECO:0000313|Proteomes:UP000070258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15929 {ECO:0000313|Proteomes:UP000070258};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:KXP12554.1}.
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DR EMBL; LSRF01000012; KXP12554.1; -; Genomic_DNA.
DR RefSeq; WP_068570535.1; NZ_LSRF01000012.1.
DR AlphaFoldDB; A0A138AQ34; -.
DR STRING; 239498.AXK60_04890; -.
DR Proteomes; UP000070258; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR046667; DUF6537.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 483..574
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 758..944
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 989..1185
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 128902 MW; 32F1A886B5F9E788 CRC64;
MTLDANSPID KLPGTAGEAA EGQHDADPRG GQSAAVQSFS LDDRYTREEG TIYLTGIQAL
VRTVRDRARL DRRQNLKTGS FISGYEGSPL AGYDLEIAKR GKYLQDFDTV HRPGLNEELA
ATSVMGSQIA AQVGHLARGL DGVTGYWYGK APGLDRATDA LRHANMIGTH PTGGAVALVG
DDPGAKSSTV PCASEMALAD LYMPILYPAD SQDILDLGVH AAIMSRVSGL WTSLKISAHV
ADGSSTADVH PDRILPVYGD LGTSPHVPSG QLLGAKLMEL EQNQLTVRMP RATEYARINR
LNRITVRSSD DRIGIVCAGK TYLDVRESLR LIGIEDDELN GLGIRILKMG MVYPFERQIM
HEFIDGLDEV IVVEEKRDFL ETMMRDILFR HPGAPNIVGK THEDGSTLFS RFGELDVDSV
SRGLAARLAR VHGVAAAKDW LDRKAQVRTR IELPLAARSP YFCSGCPHNT STKVTDDTLV
GAGIGCHAMV LLMDPQQVGE VTGVSQMGGE GAQWVGMAPF VDEKHFVQNI GDGTFMHSGS
LALRQSVASG ERITYKLLFN GTVAMTGGQD PVGQMSLPQI CALLQAERVA KIIVTSDNPK
QTAVGLPKGI EVRDRADMLD VQRELAEVPG VTVLVHDQYC AAEKRRKRKR DKYPTPNRRV
VINERLCEGC GDCGQKSNCL SVHPVETEFG RKTRIDQSSC NLDFSCLKGD CPSFVTVTPG
VQGKIRKSVP DISAESIPQP KKARREADGM AIRVTGIGGT GVVTVSQIMA TATVLDGHSA
RTVDMTGMAQ KGGAVVSDIK VSATYVDQAA KVASGDCDVY LSCDSLVGVD PANLKVASPE
RTTSIVSTTE VPTGQMVIDT SVGYPDARSI HQAIDRASLR TVYLDPGDLT LQLFGDEQYA
NLFMVGAAFQ TGALPISSAS LERAIELNGV AVEKNLQAFR RGRQSVSDPA GVRAAIDALH
PLPAPIAASA YASAQAAKLD GASPEVLRQV ALRVDELVAY QDKAYAERYM DDVARVFRAE
KSWGSEDLTA AVAHNLHKLM AYKDEYEVAR LSQDAGFAAT VADEFGADAK KAIRLHPPTL
REMGLKNKLA LGEWVNPGMK TLAKMKRLRG TKLDFFGMTE MRKMERTLVA EYRALVGLMI
AAAEGGRVAE DQRAQVVALA ELPDMVRGYE SVKTDNVEKY RAAVQAQLEK LGW
//
