ID A0A0P1LCI6_9BACT Unreviewed; 644 AA.
AC A0A0P1LCI6; A0A0N7MQJ7; A0A0N7MYE7; A0A0P1LNK1; A0A0P1P844; A0A0S4MV79;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:CUU02259.1};
GN ORFNames=JGI4_00462 {ECO:0000313|EMBL:CUU02259.1};
OS Candidatus Kryptonium thompsoni.
OC Bacteria; Candidatus Kryptonia; Kryptonium.
OX NCBI_TaxID=1633631 {ECO:0000313|EMBL:CUU02259.1, ECO:0000313|Proteomes:UP000182011};
RN [1] {ECO:0000313|EMBL:CUU02259.1, ECO:0000313|Proteomes:UP000182011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JGI-4 {ECO:0000313|EMBL:CUU02259.1};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FAOP01000003; CUU02259.1; -; Genomic_DNA.
DR RefSeq; WP_047134736.1; NZ_CZVS01000047.1.
DR AlphaFoldDB; A0A0P1LCI6; -.
DR STRING; 1633631.GCA_001442925_00463; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000182011; 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 NCBIfam; NF041170; Oxoac_fdxalpha_Archa; 1.
DR PANTHER; PTHR32154:SF16; PYRUVATE FLAVODOXIN_FERREDOXIN OXIDOREDUCTASE DOMAIN PROTEIN; 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 Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000182011}.
FT DOMAIN 15..218
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 254..501
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 528..605
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 644 AA; 71927 MW; 2186709EE274938B CRC64;
MKINQLSWMI GGPQGSGVDS GANIFSRACA YGGLHVFGKR EYHSNIKGEH SNYVVRVDSK
PIRSHLDEID FLVTFDPETL FRHVHKVVPG GVIIYDVNQE GITVDKIPTI DKQANRRIKS
FLSENGVGYS VKDVIEYASR NGILTYGIPY VKLLEGLAEE LGDPRIARMD VMINVMAVAS
SFALLQYDFA PIERAINYVF KAKEKVAKLN IEAAKYVYKY VLENFERTSY KLEPVSKSED
GRIIIQGYQA SALGKIAGGC RFQSYYPITP ASDESVYLED NAVFEIIGEN GELEKGSIVV
VQTEDEIAAI AMAIGAGLAG VRASTATSGP GFSLMAEGLG WAGMNEVPVV VTLYQRGGPS
TGLPTRHSQE DLLFAVYAGH GEFPRIVYAS GDVEEVFYDV AKVFNFAERY QTPVIHLIDK
GMANSIMTVK KFDLSKVKID RGELVETFVD GVYKRFKFTE TGVSPRVKLG TENVVFWNTG
DEHDELGHIT EDHEVRTMMV DKRMKKLELA LQEIDDEDKA LFYGDDDADY VVLSWGSTKG
VILDAMDMLK KDGYKLKFVQ VKLLHPFPSD RVSELIGDAR FLIDIEHNKT AQFGSIVKRE
ILRDIDYYIL KYNGRPMSLS EVYMALKLIF ENKANKIQVL NNGD
//
