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
//