ID   A0A1B0ZLI5_9RHOB        Unreviewed;      1141 AA.
AC   A0A1B0ZLI5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=MFS transporter {ECO:0000313|EMBL:ANP35006.1};
GN   ORFNames=JL2886_00070 {ECO:0000313|EMBL:ANP35006.1};
OS   Phaeobacter gallaeciensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=60890 {ECO:0000313|EMBL:ANP35006.1, ECO:0000313|Proteomes:UP000092565};
RN   [1] {ECO:0000313|EMBL:ANP35006.1, ECO:0000313|Proteomes:UP000092565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL2886 {ECO:0000313|EMBL:ANP35006.1,
RC   ECO:0000313|Proteomes:UP000092565};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP015124; ANP35006.1; -; Genomic_DNA.
DR   RefSeq; WP_065270192.1; NZ_JARCJB010000011.1.
DR   AlphaFoldDB; A0A1B0ZLI5; -.
DR   PATRIC; fig|60890.4.peg.65; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000092565; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster 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; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; 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.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000092565};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          627..658
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1141 AA;  124902 MW;  12904CBA379D24B6 CRC64;
     MSTQKISLND KYDLSKSPVM LNGTQALVRL MLMQKARDTA AGLNTAGLVT GYRGSPLGAV
     DMQMSRAEKQ LKEADVTFQY GLNEDLAVTA LWGAQQAEIR GEGKFDGVFG LWYGKGPGVD
     RAGDAFRHAN MAGSSKNGGV LVAMGDDHTG ESSTVLHQSE WALMDAYLPI LSPAGVQEIL
     DFGLYGYALS RFSGLWVGLK TMKDTIEVTS VVDASPDRVK LVTPDFAMPQ DGLNIRLVDD
     RFQQEDRIID QKRFAAEAFS HANKMDKRIW GKPGAKIGFV AAGKNWLDLV HAMSLLNIDE
     AMAERLGITT YKVGQVWPLD MKGFHDWAEG LDLIVVVEEK RKLIEVQIKE AIFDDRRGRR
     VYGWHKGGGA GSMHGPELFP TRYALDPIMI AEKLGEILIE EGRDTEAIRA GLASLDEARR
     ADNAEEIAAR LPYFCSGCPH NSSTKIPEGS RAYAGIGCHF MVQWMDRETM GFTHMGGEGA
     NWIGEAPFSK RKHVFQNLGD GTYNHSGVQA IRAALAEGTN ITYKILYNDA VAMTGGQGNE
     GGLSAYRIAH ELKAMGVEHL AIVYDEKEEI DFKQFPAGVP THERAELMNV QKQMEEVEGV
     SAIIYVQTCA AEKRRRRKRG LFPDPDQRVF INSDVCEGCG DCGVQSNCVS IVPKETELGR
     KRAIDQSSCN KDFSCLNGFC PSFLTIEGAK IRKEATAELK LPDLPMPDLP KIDGTHNVVI
     TGVGGTGVVT IGAVLAQAAQ IDGKGAGMME MAGLAQKGGA VHIHCRIAET PDDISAIRVA
     TGEAHALIGG DLVVSAGAKT IGLMRTGQTG GVVNSHEIIT GDFTRDTNFQ LPTDRLEVAL
     EARLRERLDM FDASQLAQAT MGDSIFSNMM VFGGAFQRGL IPVSLEAITQ AIELNGAAVE
     KNLRAFEIGR WAVLHPEEVA KLIKPANVVE LPKTLDEKIA YRQDHLTAYQ GKGLVKRYMK
     LLDGIDDARL KEAVAKGYHK LLAYKDEYEV ARLLLSSREK AEAQFEGDLK ISYNLAPPIL
     GGVDANGRPK KRRFGPSMER GLKLLAKFKG LRGTPLDIFG YTAERKMERA LIKQYERDMK
     EWLAKASPEI MDPLVALAEL PLQIRGFGPV KMESEQKAAK RREELLAVLR QGGAPMKKAA
     E
//