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
//