ID A0A0B4BG10_9RHOB Unreviewed; 1134 AA.
AC A0A0B4BG10;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KIC46227.1};
GN ORFNames=RA29_19880 {ECO:0000313|EMBL:KIC46227.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC46227.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC46227.1}.
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DR EMBL; JWLL01000015; KIC46227.1; -; Genomic_DNA.
DR RefSeq; WP_039689331.1; NZ_JWLL01000015.1.
DR AlphaFoldDB; A0A0B4BG10; -.
DR STRING; 1577905.RA29_19880; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000031171; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; 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 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 SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:KIC46227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031171}.
FT DOMAIN 625..657
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1134 AA; 122544 MW; 20F44A72D2DD1B27 CRC64;
MSDPSHRFDT YALTDRYDRT AGRVFLTGTQ ALVRIMLDQA RRDRAAGRNT GGFVSGYRGS
PLGGLDMELW RARDRTAAAD ITFMPAVNED LGATAVLGAQ QAVLDPNCTR EGIFSMWYGK
GPGVDRSGDA LKHGNAYGSS PLGGVLVVAG DDHGCVSSSM PHQSDVAFMA WFMPTLNPAS
VEEYLSFGAW GIALSRFSGT WVGFKAISET VESGASVVLP PDPVFAQPDY TAPPGGLHIR
PSDLPSPEIE TRIGHKLEAV QAFAEANPID RRIYDVPCAP FGFVTTGKAH LDLMEALRLL
GLDEATCRAR GIDIYKVGMV WPLALRDARA FVRGKREVMV IEEKRGIIES QFKEAFYDLP
RDIPERMVGK HDETGAPLVP WTGELSPRLL APLVARRLDA FVPDLDLPAR AKALQVPPKL
LSVEGATRTP YFCSGCPHNT STKVPEGSKA ASGIGCHVMA SWMDRETGGY AQMGGEGVPW
VAASKFNGGK HIFQNLGEGT WYHSGALAIR QAVAARTNIT YKVLYNDAVA MTGGQPVDGP
VSVEAIAWSS RAEGVDRIAL VSDDVGKFDR GAFPPGTTFH DRAALDAVQR ELRDIPGVTV
LIYEQTCATE KRRRRKRGTL PTVKTFAVIN PEVCEGCGDC SVESNCLSVE PLETPLGRKR
RINPSTCNAD MSCLQGFCPS FVTVEGAARR APEPVAFDVE AALSGIPQPE LPALDAPYDL
LVTGVGGTGV ITVGALVTMA AHLEGRGASV LDFTGFAQKF GTVLSYIRLG RSPDMLHQVR
IEEAAADAVI GCDIVVSSAP KASAHYHSGT RMALNRAEMP TGDLVLHRDA SLRVDVREGA
IAEVIGSQNL AAFDANALAE RYLGDSVFAN VMLLGAAWQR GLVPVSEVAL KQAIRLNGVA
VDQNTRAFDL GRIWASDPSV LAPSAPAKTP DTADEIIAHR SQLLVDYQDA GYAARYREAL
ASHTAAFSED GRKIAARALY KLMAYKDEYE VARLHVDTGF YDSLSDQFTG DFAVHHHLAP
PLLSWRKDAR GRPVKRTFGP WMHRAMRLLA KGKGLRGTWA DPFGYTAERR EERALIDWYI
AGLERLSQGT ADANAARTFL SAPLEFRGYG PVRAEAVARL KPEADAALER ASSR
//
