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Database: UniProt/TrEMBL
Entry: A0A0E3JNV3_CLOSL
LinkDB: A0A0E3JNV3_CLOSL
Original site: A0A0E3JNV3_CLOSL 
ID   A0A0E3JNV3_CLOSL        Unreviewed;       396 AA.
AC   A0A0E3JNV3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:AKA69679.1};
GN   ORFNames=CSCA_2554 {ECO:0000313|EMBL:AKA69679.1};
OS   Clostridium scatologenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1548 {ECO:0000313|EMBL:AKA69679.1, ECO:0000313|Proteomes:UP000033115};
RN   [1] {ECO:0000313|Proteomes:UP000033115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25775 {ECO:0000313|Proteomes:UP000033115};
RA   Xie J., Zhu Z., Guo T., Song T.;
RT   "Complete Genome Sequence of the Malodorant-Producing Specialist,
RT   Clostridium scatologenes ATCC 25775.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKA69679.1, ECO:0000313|Proteomes:UP000033115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25775 {ECO:0000313|EMBL:AKA69679.1,
RC   ECO:0000313|Proteomes:UP000033115};
RX   PubMed=26210291; DOI=10.1016/j.jbiotec.2015.07.013;
RA   Zhu Z., Guo T., Zheng H., Song T., Ouyang P., Xie J.;
RT   "Complete genome sequence of a malodorant-producing acetogen, Clostridium
RT   scatologenes ATCC 25775(T).";
RL   J. Biotechnol. 212:19-20(2015).
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DR   EMBL; CP009933; AKA69679.1; -; Genomic_DNA.
DR   RefSeq; WP_029161716.1; NZ_CP009933.1.
DR   AlphaFoldDB; A0A0E3JNV3; -.
DR   STRING; 1548.CSCA_2554; -.
DR   KEGG; csq:CSCA_2554; -.
DR   HOGENOM; CLU_002569_5_0_9; -.
DR   Proteomes; UP000033115; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; 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   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   Pyruvate {ECO:0000313|EMBL:AKA69679.1}.
FT   DOMAIN          17..240
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          263..368
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   396 AA;  43834 MW;  D31C3AF6E9AB15EC CRC64;
     MKSNIKRMSG CVATANAIKL ANVDVICSYP IRPYTGIMSE LSRMVADGEL DAEFVLGEGE
     HGQLSVVYGA AAAGARAFTG SSGVGVTYAM EVYSPISGER LPLQMAIADR TLDPPGDFGS
     EQTDALCCRD QGWIQGWAST PQEALDMSLM YYRIGEDPRV LLPQYACQDG YFVSHILGEV
     DVPSQEQVDS FLPPYKNHHV LDTRNPQIIG AQMEPEMGPG TQYQRHLAVE GTYKVIEEVH
     DEFGRIFGRK YNPWLEEYMT DDAECVIFMQ GGHAETAKNV AKHLRNLGEK VGVVRLRTFR
     PFPTQQVRDV LRKFKVVGVV DNSVNFGISC GSGVLLTEAR AALYNNDEKV KTVGFVAGLG
     GSMITHDEFY KMFNILKEVN KTGKVDKQSY WAPFEL
//
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