ID Q2RSB0_RHORT Unreviewed; 1168 AA.
AC Q2RSB0;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase {ECO:0000313|EMBL:ABC22985.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:ABC22985.1};
GN OrderedLocusNames=Rru_A2185 {ECO:0000313|EMBL:ABC22985.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22985.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC22985.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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DR EMBL; CP000230; ABC22985.1; -; Genomic_DNA.
DR RefSeq; WP_011390034.1; NC_007643.1.
DR RefSeq; YP_427272.1; NC_007643.1.
DR AlphaFoldDB; Q2RSB0; -.
DR STRING; 269796.Rru_A2185; -.
DR EnsemblBacteria; ABC22985; ABC22985; Rru_A2185.
DR KEGG; rru:Rru_A2185; -.
DR PATRIC; fig|269796.9.peg.2279; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_009166_1_0_5; -.
DR PhylomeDB; Q2RSB0; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR046667; DUF6537.
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; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF02775; TPP_enzyme_C; 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.
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:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABC22985.1}; Pyruvate {ECO:0000313|EMBL:ABC22985.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 465..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 737..921
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 951..1150
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1168 AA; 125645 MW; B2C4C96FA4880DC7 CRC64;
MTIQAPINRS ELSPQAFAPE LEDKYALTGG RAYMTGTQAL VRLALAQRRS DRKAGLDTRG
FISGYRGSPL GGFDKELWKA RPWLEAEGIV FKPGINEDLA ATAVWGSQQV GLFKGARQQG
VFGIWYGKGP GIDRSGDVFK HANNAGTAPL GGVLLIAGDD HAAKSSTAAH QCEYSFMDAM
IPVLHPAGLE EVISFGLFGL ALSRYSGCWV ALKTIAETVD SSAPVLLDPD PPAFLLPAEG
QAPVGGLHIR WPDPALDQEA RLMRHKLYAA LAFARVNRID KVVMDSPVPR LGIVSVGKAY
LDVRQALDDL GIDPAMAAAI GLRLYKVGMP WPLEREGVRA FAEGLEEILV VEEKRAVVEN
QIKEQLYNWR EDVRPRVVGK FDESGAWLLP SAGELTPAMV ARALAGRIGR FVTGPSIRDR
LDWLERKDAA LAGPTAVLKR LPTYCAGCPH NTSTTLPEGS RALAGIGCHY MVTWMPERAT
ATFSQMGGEG VAWIGQAPFT DEPHVFVNLG DGTYFHSGIL AIRAAVAAGV NVTYKILVND
AVAMTGGQPI DGLLSVDGLS RQLEGEGVGK IVVVSDEPGK YPIGTVFAAG VTIRHRDDLD
AIQKDLRGWP GVSAILYDQT CAAEKRRRRK RGLLADPDRR VFINDLVCEG CGDCGKVSNC
VAIEPLETEF GRKRSVDLSA CNKDYSCLKG FCPSFVTVSG AEVRRPEGVG EVAFPPLPEP
RLADLGAPYS ILVTGIGGTG VVTIGALLGM AAHLEGKGVT VLDQTGLAQK NGAVTTHVRI
AASQEALHAV RIAAGNANLL LGCDALTAAG PEVLAKARPR ATDAVINTRP VMTAAFTRDP
DSRYPEAEVR AALSATTRRA FFLDATTIAT ALMGDSLATN PFMIGYAWQK GLLPLGRAAI
ERAITLNGAA VAFNLEALLW GRRAAHDLEA VTALLDRAGG GPEHHRRSES VAETIERRAT
FLAAYQNAAL AARYRRLVEA VVAVEKRVRP GGEALSEAVA KAYFKLLAYK DEYEVARLYS
DGRFAQALAA RFSGKPRLTV HLAPPLMSPR DPTTGRLRKR AFGAWIFPLF RLLARLKGLR
GTPFDPFGQT SERRLQRRLI TEYETTLGVI LERVDPQGYD LAVEIAGLPL EMRGFGPVLV
EAVTKAQARE RTLLAAFLAP RPLASAAE
//
