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Database: UniProt
Entry: A0A366H1R6_9BURK
LinkDB: A0A366H1R6_9BURK
Original site: A0A366H1R6_9BURK 
ID   A0A366H1R6_9BURK        Unreviewed;      1123 AA.
AC   A0A366H1R6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:RBP34118.1};
GN   ORFNames=DFR37_12422 {ECO:0000313|EMBL:RBP34118.1};
OS   Eoetvoesiella caeni.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Eoetvoesiella.
OX   NCBI_TaxID=645616 {ECO:0000313|EMBL:RBP34118.1, ECO:0000313|Proteomes:UP000253628};
RN   [1] {ECO:0000313|EMBL:RBP34118.1, ECO:0000313|Proteomes:UP000253628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25520 {ECO:0000313|EMBL:RBP34118.1,
RC   ECO:0000313|Proteomes:UP000253628};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) 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:RBP34118.1}.
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DR   EMBL; QNRQ01000024; RBP34118.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366H1R6; -.
DR   Proteomes; UP000253628; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; 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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:RBP34118.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253628}.
FT   DOMAIN          658..845
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          902..1097
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1123 AA;  121793 MW;  AAF22DA4CD654DA5 CRC64;
     MLKQHGVIHL PGQNEELAAT TLMGTQMIDE HPHPDVDGVV AYWYGKGPGL DRAGDALKHG
     NFAGTSTHGA VVILSGEDHE AKSSTVPYQQ EFAFEHHGIP VLYPSSVSEF IEFGLHAAAM
     SRYSGCWVAL KLVAPLCDGG EVVQFSPDQH RVRIPDLDID GKPFAKVANF TFFPGLNIET
     ERQLYIERHA AVQAYARENR LNRISIQSDH DSIGIVSAGK TYSDTRQALR DMGFGDEELR
     GAGIRLAKIG LLCPLDMGFI REFATGLSTV IVIEEKRDFL ERQIGHALCS VGSPKLVGKY
     DVHGKNLFPV EGGLNSDLIA TLLGRALEAI RPLPTLGNLR LAELREIAAR NYGVQPRRTL
     NYCSGCPHNV STKLAPGQIA WGAPGCHIFA AVMDTPDKRI EAVTQLGGEG LPWIGLSPFT
     TRKHIVQNIG DGSLMHSSYQ NIRFAVTAGV NITFKILFNG VIANTGGQTS IGAPSLVNLI
     SHLALEGLAK IVLIAKEPQR YKGITLPSIV SLRPSDRLEA SMMELAGVVG TTVLIYDGEC
     ANERRRRQKR GKAPAPTRFT VVNEDVCENC GDCGRKANCM SLQKVDTEFG AKTQIHQSSC
     NQDQACINGE CPSFVTVEVP AGTNIRKPTP PAFDDVFLPN PVLPSLSRPY SIYIPGLGGT
     GVITANAILA QAAFLDGNEA KSYDQTGAAQ KWGAVLSSLI VSTGANPPLT NRVGLGKANL
     YLALDLLAAV DKHNLDCCSS SHTRAVINAG LLPSGEMIRN PHLAMPGANM ISTIRAATDS
     GHTVVVDARK IAEGLFGDYM MANMVMIGAA YQAGLLPITA ESIEDAIRLN GTQAQANILA
     FRAGRLAHHA PAEISKRMIA PFRALADRTV ERKARYPRGD VRVNELVSSL LPAELALDSN
     LTSLIHTRTA DLIDYQNVAY AKRYLKIIAD VAGAEKSALG LGSGLSVTDA VARNLHKLMA
     YKDEYEVARL LLMSTFSKRV QEMFTGSVRM VFNLQPPFLR WFGLNGKVGM GPWIRPLLKI
     LSAMKFVRGT AFDPFGYLQV RRQEQELIRW YNGLIQTAMG RLTLGNQSIV LELLSLPEQI
     RGYESVKAKA IKETKEKAAD LVVQLGGGGT NRQIRSLKRN SIA
//
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