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Database: UniProt
Entry: A0KN14_AERHH
LinkDB: A0KN14_AERHH
Original site: A0KN14_AERHH 
ID   A0KN14_AERHH            Unreviewed;      1181 AA.
AC   A0KN14;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   Name=nifJ-2 {ECO:0000313|EMBL:ABK39340.1};
GN   OrderedLocusNames=AHA_3174 {ECO:0000313|EMBL:ABK39340.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39340.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39340.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC   KCTC 2358 / NCIMB 9240 / NCTC 8049
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Oxidoreductase required for the transfer of electrons from
CC       pyruvate to flavodoxin. {ECO:0000256|PIRNR:PIRNR000159}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + 2 H(+) + oxidized [flavodoxin] + pyruvate = acetyl-CoA +
CC         CO2 + reduced [flavodoxin]; Xref=Rhea:RHEA:44140, Rhea:RHEA-
CC         COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000159};
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}.
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DR   EMBL; CP000462; ABK39340.1; -; Genomic_DNA.
DR   RefSeq; WP_011706951.1; NC_008570.1.
DR   RefSeq; YP_857665.1; NC_008570.1.
DR   AlphaFoldDB; A0KN14; -.
DR   STRING; 380703.AHA_3174; -.
DR   EnsemblBacteria; ABK39340; ABK39340; AHA_3174.
DR   KEGG; aha:AHA_3174; -.
DR   PATRIC; fig|380703.7.peg.3168; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1013; Bacteria.
DR   eggNOG; COG1014; Bacteria.
DR   eggNOG; COG1149; Bacteria.
DR   HOGENOM; CLU_002569_0_0_6; -.
DR   OMA; NTVMQVC; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000000756; Chromosome.
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:0043873; F:pyruvate-flavodoxin oxidoreductase activity; IEA:RHEA.
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:ABK39340.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN          685..714
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          741..771
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         27
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         60
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         110
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         694
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="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="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         704
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         750
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="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         756
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         760
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         824
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         827
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         829
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         852
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT   BINDING         852
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         970..973
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT   BINDING         999..1004
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
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            27
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            60
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT   SITE            110
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;  129441 MW;  58779AFE1AE160F3 CRC64;
     MITTDGNNAV ASVAYRTSEV IAIYPITPSS SMAEQASAWS SERGLNLWGD VPRVVEMQSE
     GGAIAAVHGA LQTGALATSF TSSQGLLLMI PNLYKLAGQL IPFVLHVAAR TVATHALSIF
     GDHSDVMAVR QTGCALLCAS NVQEAQDFSL IAQVASLNSR LPFIHFFDGF RTSHEIAKIV
     PLDDDTLRAL LPAEAIRAHR ERALTPDKPV IRGTAANPDT YFQCREATNP WYDDGYRHVS
     EAMDAFGERT GRHYRPFEYV GHPEAERVLV LMGSAIGTCE EVITRLIAQG EKVGVVKVRL
     YRPFSAAHLL AVIPESARKI AVLDRTKEPG ALAEPLYLDV MSALAEAVSR GDRASLPRVI
     GGRYGLSSKE FNPACVQAIF DELALDNPRP RFTVGIFDDV TGLSLPLPAL DYSSPGLGNQ
     HKLEALFYGL GSDGTVSAAK NSIKILGNHT DLYPQGYFVY DSKKAGGLTV SHLRVGERPL
     QSAYLVDEAD FIGCHQWQFI DMYQMAERLR PDGIFLLNSP YDAGQIWQRL PQEVQQALLQ
     KRARLYTINA AKIARECQLG NRINTVMQMA FFQLTAIIPP AEATELLRQT IASSYGSKGQ
     TLVERNWQAL AATCEALVQV PLQALDPASH QRPPVVSTKA PDFVQTVTAA MLAGLGDSLP
     VSAFPPDGTW PVGTTRWEKR NIAKEVPIWQ ADLCTQCNYC VAACPHSAIR AKVVDKEALE
     QAPATLDALD VKARDMRGQQ YVLQVAPEDC TGCNLCVEVC PAKDRTEPSR KAINMESRLD
     HLEAQKANYD FFLDLPERSA EQLERIDIRT SQLISPLFEY SGACSGCGET PYIKLLTQLY
     GDRLLIANAT GCSSIYGGNL PSTPYTTNAD GRGPAWANSL FEDNAEFGLG FRLTVDQHRE
     RVRRLLASLG DAVPAELQQG LQDTSLPVSE QRAHIEQLRD LLQGRTDAAA QELARDADYL
     VEKSVWLIGG DGWAYDIGYG GLDHVLSLGE NINVLVLDTQ CYSNTGGQQS KATPLGAITK
     FGEQGKRKGR KDLGANVMMY GHVYVAQISL GAQMNQTVKA IQEAEAYPGP SLIIAYSPCE
     EHGYDLAQSH EQMKQLTATG FWPLYRYDPR RSEEGKAPLA LDSRAPSASL AETLQQEPRF
     KRLERQLPEI ASQLYREAEL DANRRFAWLS QLAGKEAPAQ E
//
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