ID   D9QSQ0_ACEAZ            Unreviewed;       393 AA.
AC   D9QSQ0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Pyruvate ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:ADL11588.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:ADL11588.1};
GN   OrderedLocusNames=Acear_0036 {ECO:0000313|EMBL:ADL11588.1};
OS   Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL11588.1, ECO:0000313|Proteomes:UP000001661};
RN   [1] {ECO:0000313|EMBL:ADL11588.1, ECO:0000313|Proteomes:UP000001661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC   {ECO:0000313|Proteomes:UP000001661};
RX   PubMed=21304692;
RA   Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA   Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT   7288).";
RL   Stand. Genomic Sci. 3:57-65(2010).
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DR   EMBL; CP002105; ADL11588.1; -; Genomic_DNA.
DR   RefSeq; WP_013277035.1; NC_014378.1.
DR   AlphaFoldDB; D9QSQ0; -.
DR   STRING; 574087.Acear_0036; -.
DR   KEGG; aar:Acear_0036; -.
DR   eggNOG; COG0674; Bacteria.
DR   HOGENOM; CLU_002569_5_0_9; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000001661; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
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   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 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:0000313|EMBL:ADL11588.1};
KW   Pyruvate {ECO:0000313|EMBL:ADL11588.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001661}.
FT   DOMAIN          16..239
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          262..366
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   393 AA;  43071 MW;  A5B7C16611F038F5 CRC64;
     MSNEVALTGH EVIANAMRQI NPDVVAAYPI TPQTEIVQLF SQFVADGKVD TDFVTVESEH
     SAMSATVGAS AGGARAMTAT AANGLALMWE IVYIAASTRL PIVMPVVNRA LSGPINIHCD
     HSDAMGARDS GWIQLYAEDA QEAYDNAVQA VRIGEHEDVR LPVMVNMDGF IISHAVENME
     LLADEDVQEF VGEYEPENTL LDSENPITVG PIDLQDFYFE HKRQQVDAME NAKDVIADIA
     QEYKEMTGRG VEYFEEYKLD DAEIGILALG STAGTAKVAV DDLREQGVKA GLLKLRMFRP
     FPTEELVEAL KDLEVLAVMD RADTFSTTGG PVFADVRSAF YDAKADVEVV NYIYGLGGRD
     TRVEDIESIY EDLQEIAASG KVENRVNYLG VRE
//