ID   A0A0U3DP96_9BURK        Unreviewed;      1183 AA.
AC   A0A0U3DP96;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:ALT79359.1};
GN   ORFNames=AT984_21340 {ECO:0000313|EMBL:ALT79359.1};
OS   Paucibacter sp. KCTC 42545.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT79359.1, ECO:0000313|Proteomes:UP000056576};
RN   [1] {ECO:0000313|EMBL:ALT79359.1, ECO:0000313|Proteomes:UP000056576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT79359.1,
RC   ECO:0000313|Proteomes:UP000056576};
RA   Kim S.-G., Lee Y.-J.;
RT   "Complete genome of Paucibacter sp. KCTC 42545.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP013692; ALT79359.1; -; Genomic_DNA.
DR   RefSeq; WP_058721821.1; NZ_CP013692.1.
DR   AlphaFoldDB; A0A0U3DP96; -.
DR   STRING; 1768242.AT984_21340; -.
DR   KEGG; pkt:AT984_21340; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000056576; Chromosome.
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; cd02008; TPP_IOR_alpha; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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   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.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:ALT79359.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000056576}.
FT   DOMAIN          483..576
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          763..950
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          977..1175
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1183 AA;  129632 MW;  1F48DDF9EA61BB33 CRC64;
     MNAPLPDHIL RALETVTLDD KYALDSGRAF MSGVQALVRL PMLQRTRDAM VGLNTGGFIS
     GYRGSPLGTY DQALQAAKKH LAKQNIVFQP GVNEELGATA VWGTQQLDLF PEKNKFDGVF
     GIWYGKGPGV DRCIDVFKHA NMAGTAKHGG VIAVAGDDHI AKSSTAAHQS DHVFKAVGFP
     VFFPTSVQDI LDMGLHAFAM SRFSGLWSGL KTIQEIVESS SSISVDPDRV KIIMPEDFQM
     PEGGLHIRWP DAPLEQEKRL MDYKWYAALA YIRANKLNYN VIETKQDRFG LIASGKAYND
     TRQALHDLGL DDDTCRRLGI RLHKVNVVWP LEATITRDFA EGLQEILVIE EKRQMIEYQL
     KEELYNWRSD VRPHVLGKFD DHEGEGGEWS LPNPSSNWLL RPQADLTPAI IARAIAKRLK
     KLGVDADVMA RLDARVAIID AKENALKAEE KTAGGADRTP WFCSGCPHNT STRVPEGSRA
     VAGIGCHYMV SWMPGRNTAT FTQMGGEGVP WVGQSAFTNE KHIFANLGDG TYFHSGLLAI
     RQSIAAGVNI TYKILYNDAV AMTGGQQVGE RAEGHTVLQI MQSVTAEGVS KLCIVTDEPQ
     KYQGVSLLAG VSVHHRDELD AVQRQFREIP GTSVIIYDQV CATEKRRRRK RGKLVDPVKR
     VLINELVCEG CGDCSVQSNC LSIEPVDTEF GRKRQINQNS CNKDYSCVKG FCPSFVTVEG
     GELKKPKKDK KLSPFDSAKL GAIPQPVVPN AEKAWGIVVG GVGGTGVITI GQLLGMAAHL
     EGKGVITQDA AGLAQKGGST WSHIQIANKA EDLHCTKVGT AEAKLVIACD SIVAANKATL
     AVMREGHTYV ALNTHGSPTA NLVNDANWSF PGAACESAVL AAVGQSHLGM FDAEEVAVKL
     VGDSLYTNPL MLGYAWQQGR IPLSYAALMR AIELNNVQID NNKIAFEWGR RCAHDLAAVQ
     ALFVATQVIN IVKRPGVEEL VSKRVAFLTD YQNAAYAAAY KALVDKVQAA EKPLGGSQLS
     EAVARYLFKL MAYKDEYEVA RLHTDKRFTD KVAAQFEGDY KIIHHLAPPL LAKKNEKGEL
     VKQQMGAWIR PAFGLLAKLK GLRGTAFDIF GHTEERKTER ALIAEYRASI EAILAKGLTA
     ERLKLAVDIA RIPEEIRGYG HVKERHLKAA RAKWASLMGQ WQA
//