ID A8B852_GIAIC Unreviewed; 1199 AA.
AC A8B852;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 08-NOV-2023, entry version 96.
DE SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:EDO81274.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:EDO81274.1};
GN ORFNames=GL50803_0017063 {ECO:0000313|EMBL:KAE8305341.1},
GN GL50803_17063 {ECO:0000313|EMBL:EDO81274.1};
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922 {ECO:0000313|EMBL:EDO81274.1};
RN [1] {ECO:0000313|EMBL:EDO81274.1, ECO:0000313|Proteomes:UP000001548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000313|Proteomes:UP000001548},
RC and WB C6 {ECO:0000313|EMBL:EDO81274.1};
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
RN [2] {ECO:0000313|EMBL:KAE8305341.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB C6 {ECO:0000313|EMBL:KAE8305341.1};
RA Xu F., Jex A., Svard S.G.;
RT "New Giardia intestinalis WB genome in near-complete chromosomes.";
RL Submitted (JUL-2019) 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 -!- 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:EDO81274.1}.
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DR EMBL; AACB02000005; EDO81274.1; -; Genomic_DNA.
DR EMBL; AACB03000001; KAE8305341.1; -; Genomic_DNA.
DR RefSeq; XP_001708948.1; XM_001708896.1.
DR AlphaFoldDB; A8B852; -.
DR SMR; A8B852; -.
DR STRING; 184922.A8B852; -.
DR EnsemblProtists; EDO81274; EDO81274; GL50803_17063.
DR GeneID; 5701866; -.
DR KEGG; gla:GL50803_0017063; -.
DR VEuPathDB; GiardiaDB:GL50803_17063; -.
DR HOGENOM; CLU_002569_0_0_1; -.
DR InParanoid; A8B852; -.
DR OMA; NTVMQVC; -.
DR Proteomes; UP000001548; Chromosome 5.
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 GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
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 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000159-50};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
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:0000313|EMBL:EDO81274.1}; Pyruvate {ECO:0000313|EMBL:EDO81274.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001548};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 697..726
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 756..790
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 706
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 709
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 712
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 716
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 767
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 770
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 773
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 777
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 837
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 840
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 865
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 1105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
SQ SEQUENCE 1199 AA; 131803 MW; 3B0688C6763294B6 CRC64;
MSVVHAPIDG CHAAAHVSYF FSDASIIYPI TPSTPMAEYV DSWAAKGRKN AFGQTLRVEE
MNSEGAAAGA LHGALSTGLL ASTYTASQGL LLMIPNMYKM AGEHLPAVFH VAARTIATHS
LSVHGDHADI MAVRQTGCTI MVSEDIQEAM DMAIAAHLTA IYSSHPVVHA FDGFRTSHTI
KKVELIDYEH LRPHVPYDEI EAFRQKSLSP QHPEMRGSCQ GPPIWMQAGE ADNKHYAEIP
GHIERAFEKV REITGRSYKF FNYFGAPDAT AVVIIMGSGY LTVREVVEYL VERGDKVGVV
CVHLFRPFCG DKLLEAIPTS CRRICVMEKA KEIMAGAEPL RLDVIEALYS GNRLSAVTTV
IGGIFGLSSK DFNTADAFAI FRNLQATTPL NNFTVGIEDD VTHMSLKRDP ASPSLVPKGT
VQCLFFGMGS DGVVGANKNA IKIISDNTPL FTQGYFDYDS FKAGGFTSAH LRFGDKPIRC
EYLIHDADFT AVSQPSYLTK YNILLVERCK PGSLLLLNTS ASNVEEVTAA IPKNMRKMIE
DKGLKLMVMD ASEISLEAGL PGRINSALQT AFFLLSGVLP PDQAIDIWKK TVIKTFSRKG
EKVVNMNLAC IDATIKEGAI KEIKYPKNWA SIEDGSFVKM YNKRMEKIVS AAPEFVKNVM
IPATTGRGDD LKVSAFRKGG FMMTGTTQYA KRNIAVQVPV WQSSTCIQCM LCVTACPHAV
IRPYLVSSEE EEKLAPVIRD QLIPIKNPVV KSKGNFKLAI QASTLDCTGC QVCSQVCPTR
EKGTLKMEVT HNVEAREVEK FYSLADNVSV KTDDWTLDES EKAYQYRRPL FEYHGACAGC
GETAYITHVT RLFGSRLIIA NATGCSSIYG FSFPFSPYTK NAKGQGPAWA NSLFEDNAEF
GMGMLVGIQQ RRERILETVK GLVAKNLGGD KFIEAANSWI ENYNKIAESE TAGDKLKEQI
MALSADCDEL REAKDLLTLP SNLDLLARPL VLIQGGDGWS YDIGFAGLDH VLSTGLDVTI
LILDTEVYSN TGGQRSKATP LGAVARFAAA GKRTEKKDMG QIAMAYDNVY VGSISLGYSH
TAAIKTIREA FEWTGPSIVM AYAPCIEHGE DMKASNATQK LAVETGYWLT YTRHPERGLV
MGCKEPSKPV TDFLNRQNRF NQLLSERPAE AEVLRTELQD FVNSRYKKYS EMQATAKAE
//