ID A0A0S9Q0F2_9ACTN Unreviewed; 648 AA.
AC A0A0S9Q0F2;
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:KQP63377.1};
GN ORFNames=ASF47_14855 {ECO:0000313|EMBL:KQP63377.1};
OS Nocardioides sp. Leaf285.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP63377.1, ECO:0000313|Proteomes:UP000051495};
RN [1] {ECO:0000313|EMBL:KQP63377.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP63377.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP63377.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP63377.1,
RC ECO:0000313|Proteomes:UP000051495};
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:KQP63377.1}.
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DR EMBL; LMNH01000004; KQP63377.1; -; Genomic_DNA.
DR RefSeq; WP_056864810.1; NZ_LMNH01000004.1.
DR AlphaFoldDB; A0A0S9Q0F2; -.
DR Proteomes; UP000051495; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:UP000051495}.
FT DOMAIN 20..212
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 261..479
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 526..589
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 648 AA; 68568 MW; 9B31B5DB4E01EDBA CRC64;
MSKQVKQLDR VIIRFAGDSG DGMQLTGDRF TQESAAFGND LVTLPNFPAE IRAPQGTLPG
VSSFQVHFAD HDILTAGDAP DVLVAMNPAA LRANLPDLPR GATIIVDTHD FGGRNLTKAG
YDSDPLADLG SPGSPLADFA VHPVDLTGMT VGAVKEFGLS RKDAARAKNM FALGLLSWMY
GRPTDSTEAF LAKRFAKVPA IRDANLAAFS AGWSFGETTE TFAVRYEVKP APMAPGTYRN
ITGNLALSYG LVAAGVQSGL PVFLGSYPIT PASDILHELS KHKAFGVTTF QAEDEISGVG
SAIGASFAGH LGVTTTSGPG VALKSEAIGL AVMTELPLVV IDVQRGGPST GLPTKTEQAD
LLQAMFGRNG EAPVPVVAPQ SPGDCFDAAL EATRIAVTYR TPVILLSDGY LANGSEPWRI
PDVEDLPRID PGFATGPNHV VSPDDPDTRD FWPYLRDEDT LARPWAVPGT PGLEHRIGGL
EKGEGHGNIS YDPANHDRMV RTRQAKVDRI AASLPPLEVD DPSGAASVLV IGWGSTYGPI
GAGVRRVRRA GHRVAQVHLR HLNPFPDDLG EILRGYDKVL VPEMNLGQLS LLLRARYLVD
AVGYNHVRGL PLKAAELAEA IGALVAEAEG VEVDLSAPAG DPADHPED
//
