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Database: UniProt
Entry: A0A0F2J1A0_9BACT
LinkDB: A0A0F2J1A0_9BACT
Original site: A0A0F2J1A0_9BACT 
ID   A0A0F2J1A0_9BACT        Unreviewed;       559 AA.
AC   A0A0F2J1A0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein {ECO:0000313|EMBL:KJR42717.1};
GN   ORFNames=MCHI_001390 {ECO:0000313|EMBL:KJR42717.1};
OS   Candidatus Magnetoovum chiemensis.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Magnetoovum.
OX   NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR42717.1, ECO:0000313|Proteomes:UP000033718};
RN   [1] {ECO:0000313|EMBL:KJR42717.1, ECO:0000313|Proteomes:UP000033718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS-04 {ECO:0000313|EMBL:KJR42717.1,
RC   ECO:0000313|Proteomes:UP000033718};
RA   Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT   "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT   conserved set of magnetosome genes.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJR42717.1}.
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DR   EMBL; JZJI01000372; KJR42717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2J1A0; -.
DR   PATRIC; fig|1609970.3.peg.1540; -.
DR   Proteomes; UP000033718; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03377; TPP_PFOR_PNO; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 4.10.780.10; Pyruvate-flavodoxin oxidoreductase, EKR domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR   InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF10371; EKR; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SMART; SM00890; EKR; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:KJR42717.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033718}.
FT   DOMAIN          54..83
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          110..139
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   559 AA;  61533 MW;  442DABDA788D349A CRC64;
     MRHAVSQDAP EFVKNVTAKI IEGYGDLLPV SAMPDDGTWP TATTQYEKRN IGLMIPVWEP
     DACIQCGTCS FVCPHATIRM KAYDPKNLEN APSTFKSADA TGKELTGLKF TIQVAPEDCV
     GCASCVDGCP GRKKDEHGKR TEVRAINMQL QEPIRHTEAE NYKFFLNLPE TDPTKYKITT
     VKGSQFVRPL YEYSGACAGC GETPYIKLLT QLFGDRLLIG NATGCSSIYT GNLPTTPYAK
     REDGRGPAWA NSLFEDNAEF ALGMRQTCDQ FNKQALELLA RLAATTHTSL SQLNEDIKNA
     DMSNQEGIEK QRARVAELKK KLEGDNSTDA KLLVSLADYL VKKSVWALGG DGWGYDIGYG
     GVDQVLASGE NINIMIMDTE VYSNTGGQMS KSTSRGAIAQ FAAGGKRNAK KNIGLIMATY
     GNVYVAQVAY GANPVQVIKA MLEAEAYNGP SLVIAYAHCI AHGIDMTKGL GTQKAVVSSG
     YWPLYRYNPE LEAQGKSPMQ IDTKEPSTEI EDFAYNENRF RALKAQEPEI AAELMKELKH
     DVSRRWDFIK HWASWQPKV
//
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