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Database: UniProt
Entry: A0A0D7EHG7_RHOPL
LinkDB: A0A0D7EHG7_RHOPL
Original site: A0A0D7EHG7_RHOPL 
ID   A0A0D7EHG7_RHOPL        Unreviewed;      1663 AA.
AC   A0A0D7EHG7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:KIZ38977.1};
GN   ORFNames=OO17_21835 {ECO:0000313|EMBL:KIZ38977.1};
OS   Rhodopseudomonas palustris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ38977.1, ECO:0000313|Proteomes:UP000032515};
RN   [1] {ECO:0000313|EMBL:KIZ38977.1, ECO:0000313|Proteomes:UP000032515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL398 {ECO:0000313|EMBL:KIZ38977.1,
RC   ECO:0000313|Proteomes:UP000032515};
RA   Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT   "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT   isolated from estuarine surface water.";
RL   Submitted (NOV-2014) 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:KIZ38977.1}.
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DR   EMBL; JXXE01000476; KIZ38977.1; -; Genomic_DNA.
DR   RefSeq; WP_044415565.1; NZ_JXXE01000476.1.
DR   STRING; 1421013.GCA_000504425_02581; -.
DR   PATRIC; fig|1076.23.peg.5130; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000032515; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 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; 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   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
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   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF12837; Fer4_6; 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   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};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:KIZ38977.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          838..868
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          969..999
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1663 AA;  179171 MW;  4621818F9C26748B CRC64;
     MNAKYPGLPS VIHGNGAVAQ VMGHVCGGVI GYPITPSTEI SEIYEAFRSA GGCNVWGKHP
     FFFEPEGEHS AQSGALGAAL TGGKFVSNAS SSQGILYGLE SHYVTVGKKV GGFVLQVAAR
     VVSKHSLNVM AGHDDVYALL SSGYTILFGA NPQEAADLAA ISYKVSATSL IPVANAMDGF
     ATSHMLSEAL MPEPELLREF LGDPAGRIKC PTVAQEMLFG AKGRVFQLKQ YLARHEGDFI
     ACDLTKLKLH LDSHADAIES DNDGALIGAT LDYVPEELRG QWKRQWINAP EKGTRQLVPA
     LVDIDNPGLT GGVQNQPDFQ AGAVDHRTHF ANAVPRFVNE AMAEFSALTG REYRPVMTYM
     CDDADTVLVG LGSVTDDAEA VATYLRSQGK KVGVVAIKLL QPFPEAELVA ALAGKKAVTV
     LERSEVTALT QFVTQALCKA RENADGVRHA GIPPIDKLPK LTTAIFGLGA HDLQPRHLIA
     AYKNMENPTT NAPFVYLGTQ FFTKTPSPRM AVLQDRLKAA YPETQFMALS TEDNPSLLPA
     SAFRIRFHSI GGYGTIASGK LLTDILAGVL ELHSKSAPKY GSEKSGSPTN YYITLSPEPI
     KITNAELEDV EIVISPDHKV FVHTSPLRGL VDGGTFILQS NLPALEVWRE LPASARNTIR
     DKNIRFFVID AFAVAKQHAP TAELETRMMG IAFIGAVCGH VDRVVADTSQ DVILTKIRQQ
     IAKKFGAKGG PVVEGNMAVI REGLEATHQV DYDAPEFRAA EVKPAAKTSH NVSTSAAMCR
     IAAPASAAGF LDPQYYDDVM AAPFRDGTIA DAPVLPGVGL FMPAGSAAMK DKGLFRRNVP
     EFNPDLCTGC LECALVCPDA AIPNAVHDIH ELLTTAIGQL DIAPAQQDAL RGQVPALTEA
     IREIYRSSKE NRTLHDVVAQ VAATSDTDNA TLKRNLSKLA AALQVYPVAR TRPFFDAMEK
     SQPGSGGLYS VSVDPWKCSG CLECIEVCGP GALVDREQDE PLLETLQTRF EFLSRMPNTP
     ARFFDGATSA GGETKRLMLD RANYYATTGG HGACRGCGEV TAIRLVTSTN HAIHDKRRRD
     HTRELEALID QLAAKRDAVA ADTERCARID RTLKTLEKRL YLYESGPTGN GPSGMVIANA
     TGCSSVYAST FPFNPYTDPW VNSLFQDAPA IAKGLFEGLT SAASDDFRAL RIARLELADA
     YDPAVHDEVL RYFGWGQFTP QERALLPTVL SLGGDGATYD IGFGALSRLL ATKTPVKVVV
     LNTGAYSNTG GQTSTASLTG QDSDLSRYGV ANHGKQESRK ELGLIAAFHP NVFVVQTATS
     LQGHFLKNVM EFLNVTDSPA VLDVYTPCQA EHGIGDAVAN RQARKAVESR MNPVFVHDPR
     RGANLRSKFS LDGNPEPDQD WASQSIEYVD DNGATQLLKT KVTPADFAFT EVRFKKQFKR
     LAKDADAVPV EDYVTLSAEQ RVGKTPFIHA TDADKHLVRY AVGDGVIQLV EERRKYWRTL
     QYLAGFEVRQ IDENHRVELE ALLQRYDESI KARESSLDSI ARGMSELAAS SNAPAAGGFA
     GLMAGLAPSA TAPMAAVNAA KSANGAGAIP ITINESDLDK CTNCKSCYQD VPEVFELTKI
     MVGGASKDVA HVIPNVFSKI KITPELTAKL NRAAANCDAE IIR
//
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