ID A0A2U1CQW5_9BURK Unreviewed; 1194 AA.
AC A0A2U1CQW5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:PVY68276.1};
GN ORFNames=C7440_0671 {ECO:0000313|EMBL:PVY68276.1};
OS Pusillimonas noertemannii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=305977 {ECO:0000313|EMBL:PVY68276.1, ECO:0000313|Proteomes:UP000246145};
RN [1] {ECO:0000313|EMBL:PVY68276.1, ECO:0000313|Proteomes:UP000246145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10065 {ECO:0000313|EMBL:PVY68276.1,
RC ECO:0000313|Proteomes:UP000246145};
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 (APR-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:PVY68276.1}.
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DR EMBL; QEKO01000001; PVY68276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1CQW5; -.
DR STRING; 1231391.GCA_000308195_03265; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000246145; 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 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:PVY68276.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246145}.
FT DOMAIN 736..923
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 982..1172
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 130641 MW; 2823250410B35087 CRC64;
MKSALKSVQS NNHESTLDAR YDPNTPNTFL NGNHALIRMM LEQMRADRNE GLRTKAFVTG
YPGSPLGSID IALKQAKPVL EAEGITHRPA QNEEFAVSML IGTQMLDEHP HPDVDGVVGY
WYGKGPGLDR SGDALKHGNF AGTSHHGAVV ILSGEDHEAK SSTVPYQQEF SFEHHGIPVL
YPSSIQEFLD YGLHAAALSR YSGCWVALKL VGTLCDGGEV VQMHPNGLTP QLPPFQPGGK
PFVRMANHRF FPVRNIETER KLYDERHAAI LAYAQANELN RIVRSSPNDR IGLISAGKSW
ADTLQALEDL GYDDAMLQAQ GIRLAKVGLL CPGEPAFFRR FAEGLETVIV IEEKRDFLER
QVAASIIGTS VREILGKHDQ LGQRLFPIEG GMTSDIVAKH LARLLSRQQA LPERGQTRIE
YLYNKTIHRP ETLPGRAPNY CSGCPHNVST LLAPGQVAWG APGCHLFAAL MDKPEKRVEA
TTQLGGEGLP WLGLAPYTSR PHIVQNVGDG ALFHSSYANI RYAIVSGANM TFKLLINGVL
ANTGGQEAIG ASAIADLTDR LLKDGAKRVV LITKEPGQYA KLSLPDELIR RPPEALEATM
KELAEINGVT IVIYDGACAN ERRRRQKRKL LPPPTIFTLV NEEVCENCGD CGAKANCMSL
QKVSTAFGTK TQIHQSTCNQ DQACISGECP SFVSVEVSPE HGLRKPKLPN IDLSQIPEVA
PIDLDSPYHV YIPGLGGSGV LTASAIIAQA AALQGLQVKT YDQTGAAQKW GAVLSSLIFT
PANQPSHTNK VGIGKADLYL ALDLLAAVDP QNLMCCDTQR TRAVINTGVF PNGEVVRDSR
RTLPVEELRD TVAAATNRKS NLMLDARRIA EALFGDFMMT NMVAIGAACQ AGWLPIDPRY
IETAIELNGV QVQANTMALR AGRLWVHDRS RVEALGSMQA APLSDRSLRL QELRTSGKLA
ALAPLEARLA GLPTEPHSRL MLRSADLVDY QNSAYAIRYL NRVIAAFDAE TLVSGQANGY
AVTSAVIDGL HKMMAYKDEY EVARLLTRST FEQRVADQFS GPVRVHYHLQ PPLARVFGLK
GKIRVGPWLR PVLKTLSNFK FLRGTAFDPF GAVAARREER ALLAWYEKLL DDALPMLKAG
NAKKVAEILR LPETIRGYET VKSANASEAQ VRAIQLLEEL QRPRRINIAV TESI
//