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Database: UniProt
Entry: A0A0G3BUE9_9BURK
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Original site: A0A0G3BUE9_9BURK 
ID   A0A0G3BUE9_9BURK        Unreviewed;      1192 AA.
AC   A0A0G3BUE9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:AKJ31648.1};
GN   ORFNames=AAW51_4957 {ECO:0000313|EMBL:AKJ31648.1};
OS   Caldimonas brevitalea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Caldimonas.
OX   NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ31648.1, ECO:0000313|Proteomes:UP000035352};
RN   [1] {ECO:0000313|EMBL:AKJ31648.1, ECO:0000313|Proteomes:UP000035352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ31648.1,
RC   ECO:0000313|Proteomes:UP000035352};
RA   Tang B., Yu Y.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP011371; AKJ31648.1; -; Genomic_DNA.
DR   RefSeq; WP_047196757.1; NZ_CP011371.1.
DR   AlphaFoldDB; A0A0G3BUE9; -.
DR   STRING; 413882.AAW51_4957; -.
DR   KEGG; pbh:AAW51_4957; -.
DR   PATRIC; fig|413882.6.peg.5171; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000035352; 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; -; 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   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 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:AKJ31648.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035352}.
FT   DOMAIN          486..635
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          762..949
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          979..1176
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
FT   REGION          725..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1192 AA;  131258 MW;  2EDC7CE2A4A3D2EE CRC64;
     MNAPLPESIR KALESVSLDD KYALDHGRAF MSGVQALVRL PMLQRTRDAR NGLNTGGFIS
     GYRGSPLGGY DQALWQAKQH LAANNIVFQP GVNEELGATA VWGTQQLDLY PEQKKFDGVF
     GIWYGKGPGV DRCSDVFKHA NMAGTAKHGG VIALAGDDHV AKSSTAAHQS DHIFKACGLP
     VFFPASVQEI LDLGLHAFAM SRFAGVWAGM KTIQEIVESS SSVSVDPDRV DIVLPEDFVM
     PPGGLHIRWP DPPLEQEARL MDYKWYAALA YVRANRLNHT VIDSPHARLG LIASGKAYND
     TRQALHDLGL DDATCRRIGI RLHKVSVVWP LEATITREFA TGLQEILVVE EKRQVIEYQL
     KEELYNWRED VRPNVLGKFS EPDGDHSGGE WSMPNPAQNW LLRAKADLNP ALIAKAIAQR
     LEKLGLMQQL DRDLRAHITS RLAIIEAKER AQAAPTVSTD RTPWFCSGCP HNTSTRVPEG
     SRAVAGIGCH YMVVWMDRQT STFTQMGGEG VPWVGQAPFT KEKHLFANLG DGTYFHSGLL
     AIRQSIAAKV NITYKILYND AVAMTGGQPV DGTMTVPQMT RELEAEGVKK MVVVTDDPAR
     YNAPLNLAPG VSVHHRDELD RLQREFREVE GCTVIIYDQT CATEKRRRRK RGTMPDVAKR
     VVINELVCEG CGDCSVQSNC LSVEPVETEF GRKRRINQST CNKDFSCVKG FCPSFVTVEG
     GQLKSAKKTG AARPDPRSLP PLPEPTLPLA ERAYGIVVAG VGGTGVITIG QLLGMAAHLE
     GKGVVTQDAA GLAQKGGSTW SHIQIANRAD AIHTTRVGTA EADLVLGCDP IVAANKTTLA
     AMVEGRTKVA LNAHGTPTAA FVHNPDWEFP GGNCDALLAQ TVGDANVGRF DADQLSLRLL
     GDSIYANPMM LGYAWQKGWV PLSHAALMRA IELNGVQVEH NKTAFEWGRR AAHDLAAVAG
     LAEPQGQVVQ FVKKQKVDLE TLIARREAFL TDYQNAAYAR RYRSFVERVR LAEAPLGSTR
     LTEAVARGLF KLMAYKDEYE VARLHTDRSF LDKIGQQFEG DYKLTYHLAP PLLAQRNDQG
     ELQKRRYGPW MLRAFGLLAR LKGLRGTALD PFGYTDERKT ERALIGQYQD TVEELLTSLT
     AERLPLAVEL ARIADDIRGY GHVKERHLVA ARAKWERLLV EWRAAAPTRQ AA
//
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