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
//