ID A0A0Q8R2G5_9SPHN Unreviewed; 615 AA.
AC A0A0Q8R2G5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Ferredoxin oxidoreductase {ECO:0000313|EMBL:KRB90096.1};
GN ORFNames=ASE22_14375 {ECO:0000313|EMBL:KRB90096.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB90096.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB90096.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB90096.1,
RC ECO:0000313|Proteomes:UP000051570};
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:KRB90096.1}.
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DR EMBL; LMID01000012; KRB90096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8R2G5; -.
DR STRING; 1736595.ASE22_14375; -.
DR Proteomes; UP000051570; 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; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
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 NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF29; BLR6743 PROTEIN; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051570}.
FT DOMAIN 23..188
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 223..386
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 615 AA; 66676 MW; 83FDE61B0A11ABD7 CRC64;
MRAMTRPIAA VNDFVVKFAN VNGSGSASAN GLFVKAILRM GVPVGARNIF PSNIQGLPTW
YEIRVSGDGW LGRRGGVDLM VAMNPQTWDR DVAEIEPGGY LFYDSTKPMP PDRFREDISI
VGIPLTALCN AAYAEPSKRK VLKNIIYLGA LTYLLGIERE VVETLLGEEY ASKPALIPAN
IEALGIGFDH AREHLAPLGL KLRRADAVGD RIFVDGNSAA GLGAVYGGAT VCAWYPITPS
TSLAEAFTAY CGKLRHDADT GEARYAIVQA EDEIASIGIV TGAGWNGARA FTCTSGPGIS
LMQEFIGLSY FAEIPGVIFD VQRGGPSTGM PTRTQQSDIL SAAYASHGDT KHVLLLPEGP
NECFEFGALA FDLADRLQTM VFVMLDLDMG MNEWLIEPFR WDEERGLDRG KIMTAEMLEG
GADFGRYKDV DGDGIPWRTL PATHPSKGSY FTRGTSRDPY ARYSEEGAVY VDNMERLLRK
FDSAKALVPP PIVRRAARQS SYGVIYYGST SPAMDEALAG LDAGGIAVDA MRLRAFPFPG
EVFEFIAAHE LVFVVEQNRD AQLRALLINE GGVDPARLVK VLNYDGSPIT ARFIQAELAK
GMGVPKARAA GEMVR
//
