ID A0A0Q7LS25_9BURK Unreviewed; 719 AA.
AC A0A0Q7LS25;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KQX91893.1};
GN ORFNames=ASD34_24655 {ECO:0000313|EMBL:KQX91893.1};
OS Variovorax sp. Root473.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX91893.1, ECO:0000313|Proteomes:UP000051275};
RN [1] {ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX91893.1, ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|EMBL:KQX91893.1,
RC ECO:0000313|Proteomes:UP000051275};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX91893.1}.
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DR EMBL; LMEV01000012; KQX91893.1; -; Genomic_DNA.
DR RefSeq; WP_056574109.1; NZ_LMEV01000012.1.
DR AlphaFoldDB; A0A0Q7LS25; -.
DR OrthoDB; 9804603at2; -.
DR Proteomes; UP000051275; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR045025; HACL1-like.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF5; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE ALPHA SUBUNIT; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:KQX91893.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051275}.
FT DOMAIN 442..587
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 719 AA; 77578 MW; CE86964F469E7344 CRC64;
MEVSFSKEVE MLRLGAGDTF HGEGILAITK GLLQSGVAYV GGYQGAPVSH LLDVMVQGKA
YMDELGVHVE ACSNEASAAA MLGASIHYPL RGAVTWKSIV GTNVAADALS NLSSPGVTGG
VLIVVGEDYG EGASVIQERT HAYALKSSMC LLDPRPDLGV MVRMVEQGFQ LSEASNMPCL
MELRIRTCHV RGSFDCKDNI APAVSTRALM NEPAGFDYMR LAHPPVTFRH EKLKGDERMP
AARRHIVANG LNELMPGRRH PDLGIVVQGG LYNALIRSLQ QQGLADAFGE TEIPILVLNV
TYPLVPEQVA DFCVGKRAVL VVEEGQPEYI EQDIATLLRR RDIQTPLHGK DLLPQAGEYG
VEVLSGGLAA FAARYLGASE AAASAQAWLA GNRERREAVA RRLDAPLPAR PPSFCVGCPE
RPVFSALKLA QQETGPVHIA ADIGCHAFGT FEPFSMGHSI LGYGMSLASR AGVAPMMNRR
TLSIMGDGGF WHNGLLTGVQ SALFNDDDAV LLIFKNGYTS ATGTQDIIST PDDEIKERAV
DKQQSLVDKN QTIEATLKGL GVQWMRTVTT YDVERMRKTL TEALTSDFNG LKVVIAEGEC
QLERQRRIKP WIAGLLKKGQ RVVRVKYGVD EDVCNGDHAC IRLSGCPTLT LKDNPDPLKV
DPVAVVIDGC VGCGLCGANA HAATLCPSFY RAEVVQNPKW HERLLHGLRS AVVSALRPA
//
