ID   L9X7W9_9EURY            Unreviewed;       584 AA.
AC   L9X7W9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein {ECO:0000313|EMBL:ELY57702.1};
GN   ORFNames=C493_07419 {ECO:0000313|EMBL:ELY57702.1};
OS   Natronolimnohabitans innermongolicus JCM 12255.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronolimnohabitans.
OX   NCBI_TaxID=1227499 {ECO:0000313|EMBL:ELY57702.1, ECO:0000313|Proteomes:UP000011602};
RN   [1] {ECO:0000313|EMBL:ELY57702.1, ECO:0000313|Proteomes:UP000011602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12255 {ECO:0000313|EMBL:ELY57702.1,
RC   ECO:0000313|Proteomes:UP000011602};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY57702.1}.
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DR   EMBL; AOHZ01000040; ELY57702.1; -; Genomic_DNA.
DR   RefSeq; WP_007258785.1; NZ_AOHZ01000040.1.
DR   AlphaFoldDB; L9X7W9; -.
DR   STRING; 1227499.C493_07419; -.
DR   PATRIC; fig|1227499.3.peg.1491; -.
DR   eggNOG; arCOG01606; Archaea.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000011602; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 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   Pyruvate {ECO:0000313|EMBL:ELY57702.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011602}.
FT   DOMAIN          13..173
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          209..454
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   REGION          409..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   584 AA;  64173 MW;  0E302E3979449404 CRC64;
     MAEDLNWAIG GEAGDGIDST GKIFAQALSR AGRHVFTSKD FASRIRGGYT AYKIRTSVDR
     VQSVVDRLDI LVALTQRTID ENLDELHDGS AIIYDGERSW EAEIPDEMTA VDVPLKSLAE
     DAGGAIMRNI VALGAACEIT GFDVEYLDES LEKRFGGKGS KIVENNKEAA RLGQEYVQEN
     YDLDHLGYSL ETTDEDYVLL NGNEAIGMGA IAAGCRFYAG YPITPATSIM EYLTGRIEDY
     GGHVVQAEDE LSAINMALGG ARAGARAMTA TSGAGIDLMT ETFGLVATSE TPLVITDVQR
     SGPSTGMPTK QEQGDLNMAL YGGHGEVPRF VVTPTSIDEC FWKTVEAFNL AEKYQTPVFL
     VSDLAMSVTE QTFRPEAFDM DEVEIDRGKL VDQDEVDEWL DEQGRFRAHA DTDDGVSPRA
     IPGTIDGAHM STGLEHDELG RRTEDQDTRV QQVDKRYRKV ETAEEQEEWE YREFGNADAD
     NLVISWGSNE GALIEALDYL EEDDIDVRVI SVPYIFPRPD LSEEMEAADD VIVVEANATG
     QFADLLEHDA LTRVKRINKY TGVRFKADEL AEEIADQLSA EVPA
//