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Database: UniProt
Entry: M1Z7Z3_9FIRM
LinkDB: M1Z7Z3_9FIRM
Original site: M1Z7Z3_9FIRM 
ID   M1Z7Z3_9FIRM            Unreviewed;       555 AA.
AC   M1Z7Z3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit {ECO:0000313|EMBL:SHD77821.1};
GN   Name=PorA {ECO:0000313|EMBL:SHD77821.1};
GN   ORFNames=CUESP1_2475 {ECO:0000313|EMBL:SHD77821.1};
OS   [Clostridium] ultunense Esp.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Tepidimicrobiaceae;
OC   Schnuerera.
OX   NCBI_TaxID=1288971 {ECO:0000313|EMBL:SHD77821.1, ECO:0000313|Proteomes:UP000245423};
RN   [1] {ECO:0000313|EMBL:SHD77821.1, ECO:0000313|Proteomes:UP000245423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD77821.1};
RA   Manzoor S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT669839; SHD77821.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1Z7Z3; -.
DR   HOGENOM; CLU_017038_1_0_9; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000245423; Chromosome chri.
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   Pyruvate {ECO:0000313|EMBL:SHD77821.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245423}.
FT   DOMAIN          11..163
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          191..428
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          454..525
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   555 AA;  61845 MW;  BD147985132B4AFD CRC64;
     MDYTVLVGGE AGQGMDTFAN LLEKILKRAG FHVFSKSDYM SRVRGGHNFI QIRFSNKPIY
     AHTEKVDIVF ALNEETVEQH LTRLKENGIV ITDEGIGKDK DLFHLPLLKT AKALRNSRVY
     TTIGLGAILK YYGLPLKTGE EVIREGFNEK LYKININALR AGYGMVDSEY SLPTLEDKHI
     LINGNQAVGL GAIAAGCKFY CGYPMTPSTG VLNYIAAHAN EMGIAVDQVE DEVAALNMAL
     GASYAGVRAM TGSSGGGFAL MVEALSLAGI IEVPVVVINV QRPGPATGFP TRTEQADLRF
     MIHAGHGEFP RMVIALRDPE DAFYQTARAF NIAEKYQIPV LLMSDQYLAD STTTREPFDF
     SKIKIERRIS GEEGVLDQEY KRYKFTEDGI SPRILPGKIP GQVVLVDSDE HDEWGNITES
     DEIRIKMVNK RMKKFEGLKE EVEEPWLLGD EKPENLIISW GSTYGPVREA VEKLLEEGIS
     IGALVFGDIW PLPTKKLMEM SKFAKRIIDV EQNATAQLDS LIREELLIKS TDKILKYDGR
     PFSGDELYTR LKEVL
//
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