ID A0A0T0PU30_9SPHN Unreviewed; 657 AA.
AC A0A0T0PU30;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KQT32415.1};
GN ORFNames=ASG29_11550 {ECO:0000313|EMBL:KQT32415.1};
OS Sphingomonas sp. Leaf412.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT32415.1, ECO:0000313|Proteomes:UP000051178};
RN [1] {ECO:0000313|EMBL:KQT32415.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32415.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT32415.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32415.1,
RC ECO:0000313|Proteomes:UP000051178};
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:KQT32415.1}.
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DR EMBL; LMQP01000003; KQT32415.1; -; Genomic_DNA.
DR RefSeq; WP_055983923.1; NZ_LMQP01000003.1.
DR AlphaFoldDB; A0A0T0PU30; -.
DR STRING; 1736370.ASG29_11550; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000051178; 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; IPR033412; PFOR_II.
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:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 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:UP000051178}.
FT DOMAIN 31..219
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 268..444
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 524..590
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 624..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 69619 MW; A00F7B5416A3CD20 CRC64;
MATAIHDVTP AESQAHPAPE SIVVRFAGDS GDGMQLTGGQ FTLSTALAGN DLATFPDFPA
EIRAPLGTLF GVSAFQINFG STAIETAGDM LDVLVAMNPA ALKTNVDALK PGGLVIADEG
EFNQRNLDKA KYTASPLDDG SLAKWQVLRL NISQLTVDAV KPFGLGNKDA LRCKNMWTLG
LSLWMFDRDR QPLVDWLKAK FAKAPMLAEA NIAALNAGHA YGETAELGGN VRQHAVAAAP
AEPGLYRTVT GAEAISLGLV AGAQLAQLPM FFGGYPITPA SAILHHLSRL KEFGVTTFQA
EDEIAAIASA IGASYAGQLG VTSSSGPGIA LKGEAMGLAI MTELPLVVVN SQRGGPSTGL
PTKTEQSDLY QAVYGRNGDA PMPVVSARSA SDCFEVAIEA VRIATTYMTP VMLLTDGYIA
NAAEPWKVPD TSTLEPFPVT FLEEAPAEGF LPYSRDEKLA RPWVKPGTPG LLHRIGGIEK
KQGTGNIDYS PANHQEMTDT RKAKVDGIVV PDQQVELGET SGKLVVVGWG STFGPIHQAV
RRARRKGVDV AHVHIRHIWP LPQNLGVLLR GYEHILVPEM NTGQLKTVLR DQYLVDAKPL
NKVSGQPFRI SEIEDAIATF FDGVPGNEGG TVPPNDVQLP GGEQGHDDGS LHGGPSA
//
