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Database: UniProt
Entry: T0ZU80_9ZZZZ
LinkDB: T0ZU80_9ZZZZ
Original site: T0ZU80_9ZZZZ 
ID   T0ZU80_9ZZZZ            Unreviewed;       299 AA.
AC   T0ZU80;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit {ECO:0000313|EMBL:EQD51851.1};
GN   ORFNames=B2A_06772 {ECO:0000313|EMBL:EQD51851.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD51851.1};
RN   [1] {ECO:0000313|EMBL:EQD51851.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD51851.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EQD51851.1}.
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DR   EMBL; AUZZ01004818; EQD51851.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0ZU80; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR011896; OFOB.
DR   InterPro; IPR032686; PFO_beta_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR02177; PorB_KorB; 1.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF12367; PFO_beta_C; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:EQD51851.1}.
FT   DOMAIN          62..209
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          213..274
FT                   /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12367"
SQ   SEQUENCE   299 AA;  32093 MW;  DDA044724A46B29F CRC64;
     MADSLVAGAK PIVGTPLPLI TKSDTKPTWC PGCGDYGVVA AIEMAVKRLG LPSHEIVIVS
     GIGCSSNLPH FLSSYGFHSI HGRALPVAEG IRWANHALTV IGTGGDGDGF GIGAGHFVHA
     MRRNVKLTYV TMDNQIYGLT TGQASPTSMM GQKTKSTPRG VIENPIDPIA LALASGATYV
     ARGFSGDVKH LADLVANGIK HKGFAFVDVM SPCVTYNKIN TFDFFRQRVY KLESSGHDPT
     NIVTAWERAL EWGEKIPIGL FYRADRPTYE ELEEVLMAGP LAQQPAGLKA HESVLDEFV
//
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