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Database: UniProt
Entry: A0A0S7YYK3_9DELT
LinkDB: A0A0S7YYK3_9DELT
Original site: A0A0S7YYK3_9DELT 
ID   A0A0S7YYK3_9DELT        Unreviewed;      1181 AA.
AC   A0A0S7YYK3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:KPJ79164.1};
GN   ORFNames=AMJ54_00470 {ECO:0000313|EMBL:KPJ79164.1};
OS   Deltaproteobacteria bacterium SG8_13.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1703398 {ECO:0000313|EMBL:KPJ79164.1, ECO:0000313|Proteomes:UP000051346};
RN   [1] {ECO:0000313|EMBL:KPJ79164.1, ECO:0000313|Proteomes:UP000051346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_13 {ECO:0000313|EMBL:KPJ79164.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000159-50};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000159-50};
CC   -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009032,
CC       ECO:0000256|PIRNR:PIRNR000159}.
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:KPJ79164.1}.
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DR   EMBL; LJNK01000001; KPJ79164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7YYK3; -.
DR   STRING; 1703398.AMJ54_00470; -.
DR   PATRIC; fig|1703398.3.peg.1527; -.
DR   Proteomes; UP000051346; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   CDD; cd03377; TPP_PFOR_PNO; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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; IPR033412; PFOR_II.
DR   InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR   InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR02176; pyruv_ox_red; 1.
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; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PIRSF; PIRSF000159; NifJ; 1.
DR   SMART; SM00890; EKR; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000159-50};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|PIRNR:PIRNR000159};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000159-50};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000159-
KW   50};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000159-50};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000159}; Pyruvate {ECO:0000313|EMBL:KPJ79164.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN          678..707
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          734..765
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         687
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         690
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         693
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         697
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         743
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         746
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         749
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         753
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         810
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         813
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         838
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         1070
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   SITE            31
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            64
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            114
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            995
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ   SEQUENCE   1181 AA;  129079 MW;  C0A5D22927B884AC CRC64;
     MAKEMKTIDG NTAAAHVAYA MSDVATIYPI TPSSPIGEIA DEWAASGRTN IFGQAMTVRQ
     MQSEAGAAAA VHGSLAAGAL TTTFTASQGL LLMIPNMYKM SGELLPGVMH VTARAVAAHA
     LSIFGDHQDV MAVRQTGFAM LASASVQEVM DLGLVAHLAS IESSIPFLHF FDGFRTSHEI
     QKIEMIDYED MAKLVNREAL ARFRARGTNP ERPELRGTAQ NPDIYFQGRE AANSYYLKGA
     GIVEAAMQQV SKLTGRTYNL FDYVGAADAD RVIVSMGSSC ETIEEVVNHL NGQGEKIGLV
     KVRLYRPFSV EHLLAVIPKT ARTIAVLDRT KEPGAIGDPL YVDVCTAFME SKQTPTIVNG
     RYGLGSKEFN PAMVKAVIDN MSAKSPKNHF TVGIVDDVTN TSLDVQPGFD VAPAGTVQCK
     FWGLGADGTV GANKSAIKII GDNTDMFAQA YFAYDSKKSG GVTISHLRFG QTPIQSTYLI
     DSADYIACHK DNYVDIYEVL EGIKQGGTFV LNSAWSLEEM EEKLPAGMRQ TIARKKLKFY
     NIDAVKIAQE VGLGGRINMI MQTAFFKLAK VLPVDEAIKL LKKEIEKMFG LKGEHIVRMN
     HEAVDKTLDK LVEIDYPASW ADVAGGPGDE RVEPDFVKNV MRPILSQQGD KLPVSAFAPD
     GIFPVDTSKY EKRGVAINVP EWIMDNCIQC NQCSMVCPHA AIRPFLVSEE EVQKAPQGFE
     AKKAVGKELK DYYFRIQVDT LDCYGCGNCA DICPSKKKAL VMKPLETQTA LQVPLWEYAV
     ELPVRDDLTK RNSVKGSQFC QPLLEFSGAC AGCGETPYAK LLTQLFGERM VIGNATGCSS
     IWGGSAPAIP YCVNRDGFGP TWGNSLFEDP AEFTYGMFLG VFQQRRKLAD LVRQALQTDV
     AADVKAALQG WLDNMKDPAG SRQYGDQLKT LLPKHKNNDL LQEINAMSKL FTKKSFWVFA
     GDGAAYDIAY GGIDHVMAAG ENINILVMDT EVYSNTGGQS SKATPTGSVA KFAFSGKKTT
     KKDMGAMMMS YGYVYVASVA MGANKQQLMK AVVEAEAYDG PSIILAYSPC INHGILRGMG
     RSQDESKLAV QSGYWPLYRY NPQLRLEGKN PFVLDSKEPD GSLKEFLSGE VRYASLKRSF
     PQEADTLQTR LEEEVAARYR QLQVMADPTA VCEQPEQQAA E
//
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