ID A0A180F3N3_9BACT Unreviewed; 1181 AA.
AC A0A180F3N3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pyruvate synthase subunit porA {ECO:0000313|EMBL:OAV66896.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:OAV66896.1};
GN Name=porA {ECO:0000313|EMBL:OAV66896.1};
GN ORFNames=Barb4_02705 {ECO:0000313|EMBL:OAV66896.1};
OS Bacteroidales bacterium Barb4.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1633200 {ECO:0000313|EMBL:OAV66896.1, ECO:0000313|Proteomes:UP000078495};
RN [1] {ECO:0000313|EMBL:OAV66896.1, ECO:0000313|Proteomes:UP000078495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barb4 {ECO:0000313|EMBL:OAV66896.1,
RC ECO:0000313|Proteomes:UP000078495};
RA Tai V., Carpenter K.J., Weber P.K., Nalepa C.A., Perlman S.J.,
RA Keeling P.J.;
RT "Genomic and NanoSIMS analyses of nitrogen-fixing bacterial ectosymbionts
RT of a protist inhabiting a wood-eating cockroach.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OAV66896.1}.
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DR EMBL; LBCX01000184; OAV66896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180F3N3; -.
DR PATRIC; fig|1633200.3.peg.1684; -.
DR Proteomes; UP000078495; 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:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
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; 1.
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:OAV66896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078495};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 681..710
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 736..767
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
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 696
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 700
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 745
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 748
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 751
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 755
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 815
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 818
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 843
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 1079
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 33
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 66
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 116
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 1004
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1181 AA; 129596 MW; D6B92C1CB95C38A8 CRC64;
MAKEKKFLTC DGNQAAAHIS YMFSEVAAIY PITPSSTMAE YVDEWAAAGR KNLFGETVLV
QEMQSEGGAA GALHGSLQAG ALTTTYTASQ GLLLMIPNMY KIAGELLPCV FHVSARTLAS
HALSIFGDHQ DVMACRQTGF AMLAEGSVQE VMDLAAVAHL ATIRSRVPFL NFFDGFRTSH
EIQKIEALAN EDLGHLIDQK ALAEFRSRAL TPEHPVARGM AENPDHFFQH KEASNAFYDA
VPAVVEEYMK ELSVITGRKY GLFDYYGAPD ADRVIIAMGS VTEAIREAID HLTAKGEKVG
LVAVHLYRPF SAKHFLAAVP KTAKRIAVLD RTKELGATGE PLYLDVKDCF YGSADAPFIV
GGRYGLSSKD TTPSQMLSVF ENLALPEPKN HFTVGIVDDV TFSSLPLKEE IALGGEGIYE
AKFYGLGADG TVGANKNSIK IIGDNTNKYC QAYFSYDSKK SGGFTCSHLR FGDTPIRSTY
LVNTPNFVAC HVQAYLRMYD VTKGLRENGT FLLNTVWTDK ELAKHLSNKA KRYFAKKNIT
VYYINATQIA QEIGLGNRTN TILQSAFFQI TGVIPAALAI EQMKKFIVKS YGKKGESIVN
MNYAAVDRGS EFQKLSIDPA WANLPDDEAT ANNDPAFINE VVRPINAQDG DLLKVSAFKG
IEDGTWMQGT AKYEKRGVAA FVPVWNKDNC IQCNQCAYVC PHAAIRPFIL DEKEQAGASF
DMLDVKAPAA FKGMKFRMQV SVLDCLGCGN CADICPGFKG AKALDMAALE TQQAEVAHWD
YCTAQVKSKQ QLIDVKSNVK NSQFATPLFE FSGACSGCGE TPYLKLISQL FGDRQIASNA
TGCSSIYSGA VPSTPYTTNE KGQGPAWANS LFEDFCEYGL GMQLANEKMR DRLVRLMRAA
IENGIPDEAR ALFEEWIENR EDAEKSKELA AKITARFEAC EGGDCGCDVL RQLKELSHYL
PKRSQWIIGG DGASYDIGYG GLDHVIASGK NVNILVLDTE VYSNTGGQSS KATPIGAIAK
FAASGKRIRK KDLGMIATTY GYVYVAQIAM GADQAQTLKA LREAEAYNGP SLVIAYAPCI
NHGLRKGMGK SQQEEADAVA CGYWHLWRYN PALEAEGKTP FVLDSKDPNW SKFQDFLKGE
VRFSSLAKQY PAEAGELFQS AEDNAKWRYR SYQRMMKQWE D
//
