ID   A0A1H1E6G2_9ACTN        Unreviewed;      1197 AA.
AC   A0A1H1E6G2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:SDQ84274.1};
GN   ORFNames=SAMN04489765_2055 {ECO:0000313|EMBL:SDQ84274.1};
OS   Tsukamurella pulmonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=47312 {ECO:0000313|EMBL:SDQ84274.1, ECO:0000313|Proteomes:UP000183053};
RN   [1] {ECO:0000313|Proteomes:UP000183053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44142 {ECO:0000313|Proteomes:UP000183053};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNLF01000002; SDQ84274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1E6G2; -.
DR   STRING; 47312.SAMN04489765_2055; -.
DR   Proteomes; UP000183053; 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   Pyruvate {ECO:0000313|EMBL:SDQ84274.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          486..624
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          762..948
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          994..1189
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1197 AA;  129518 MW;  8452B1D1444BAD69 CRC64;
     MVSVTLDANS PLQKVPDVAD ATQAGHHDAD PRGGQSAAVE SFSLDDRYTR EEGTIYLTGI
     QALVRMVRDR ARLDRRQNLT TGSFISGYEG SPLAGYDLEI AKRTKYLKDF DIVHRPGLNE
     ELAATSVMGS QIAAQVGHLD RGLAGVTGYW YGKAPGLDRA TDALRHANMI GTHPTGGAVA
     LVGDDPGAKS STVPCASEMA LADLYMPILY PADSQDILDL GVHAAIMSRV SGLWTSLKIS
     AHVADGASTA DVHPDRILPV YGDMGTSPHV PSGQLLGAKL MELEQNQLTV RLPRATEYAR
     INRLNRITVR SSDDRIGIVC AGKTYLDVRE SLRLIGIEDG ELNRLGIRIL KMGMVYPFER
     QIMHEFIDGL DEVIVVEEKR DFLETMMRDI LFRHPGAPNI VGKANEDGST LFSRFGELDV
     DSVSRGLAQR LARVHQVPAA KDWLDRKAQV RTRIELPLAA RTPYFCSGCP HNTSTKVADD
     TLVGAGIGCH AMVLLMDPQQ VGDVTGVSQM GGEGAQWVGM APFVTEKHFV QNIGDGTFMH
     SGSLALRQSV ASGERITYKL LFNGTVAMTG GQDPVGEMTL PQMCTLLLAE RVTKVVVTSD
     DPKRTKALGL PKGVEVRDRA DTLDIQRELA ELSGVTVLVH DQHCAAEKRR KRKRGKYPTP
     NQRVVINERI CEGCGDCGQK SNCLSVHPVE TEFGRKTRID QSSCNLDFSC LKGDCPSFVT
     VTPGEVGKVR KSVPDITAES IPQPKKARRE ADGMAIRVTG IGGTGVVTVS QILATATVLD
     GHSARTVDMT GMAQKGGAVV SDIKVSATYV DQAAKVASGD CDVYLSCDSL VGVDPTNLKV
     ASPERTTSIV STTEVPTGQM VIDTSVGYPD ARSIHEAIDR ASLRTVYLDP GELTLQLFGD
     EQYANMFMVG AAFQTGALPI SSTSIERAIE LNGVAVEKNL QAFRRGRQSV SDPAGVKAAI
     DALHPVPAPA PVSAFAKGLV GVLDGGSEEL LRQVGIRVDE LVAYQDKAYA ERYVDDVARV
     FRAEKSWGSE DLTAAVAHNL HKLMAYKDEY EVARLSQDAG FAAQVADEFG ADAKKAIRLH
     PPTLREMGLK NKLALGEWVN PGTKTLAKMK RLRGTKLDFF GMTEMRKMER TLIAEYRALV
     GLMIAAAEGG RVAEDQRMQV VALAELPDMV RGYESIKTGN VEKYRAAVQA QLQTLGW
//