ID   A0A261U0P3_9BORD        Unreviewed;      1165 AA.
AC   A0A261U0P3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:OZI55526.1};
GN   ORFNames=CAL25_03785 {ECO:0000313|EMBL:OZI55526.1};
OS   Bordetella genomosp. 5.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395608 {ECO:0000313|EMBL:OZI55526.1, ECO:0000313|Proteomes:UP000216913};
RN   [1] {ECO:0000313|EMBL:OZI55526.1, ECO:0000313|Proteomes:UP000216913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU10456 {ECO:0000313|EMBL:OZI55526.1,
RC   ECO:0000313|Proteomes:UP000216913};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) 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:OZI55526.1}.
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DR   EMBL; NEVP01000001; OZI55526.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261U0P3; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000216913; 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; 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; 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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:OZI55526.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216913}.
FT   DOMAIN          728..915
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          944..1144
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1165 AA;  125474 MW;  CFBD14A6F52A4E27 CRC64;
     MDGTPAVEPS LDSDYQLSDN LVRERGRIFL TGTQAIVRMV LAQRRADRAR GLNTAGFVSG
     YRGSPLGGVD MAMWKAQKAL DAHDVTFMPG INEDLAATAV MGTQQAGMRE DRKVDGVFAL
     WYGKGPGVDR AGDALHHGNA AGASRHGGVL LVVGDDHTAV SSSIPHASET SLIGWQIPIV
     HPASIDEYET FALWGWALSR YSGSWVALKA TSESVETGQS YVSAPPARFD MPDDGEAAER
     EYNARDFLSL AIETRMHRRL AAVRAFARTH SLDRLIAPAP QARVGIVTAG KVTLDTLEAL
     ARLGIDVHAA QSPVRVYKPG LVWPMDRERL LAFAQGLTHI LVIEEKAGVM EPQIKDMLFN
     LPDRPTVCGK TGLDGETLIT TAGQLRPSQL AAPLASWLGR TLGLHANVDG EAFACPQPLA
     NEADGMRRRP YFCSGCPHST STKVPKGSQA LSGVGCHYMA AWMERDTGGL TQMGGEGVDW
     IGLSRYIDTP HVFQNMGEGT YYHSGYLAIR QAVAAGTNIT YKILFNDAVA MTGGQPVDGP
     ISVPQICQQL RGENVARIVV TSDEPEKYRG VDLAGVPVHH RRELDALQRE LRATPGVTVL
     IHDQTCAAEK RRRRKKGQFP DPARRMLINA AVCEGCGDCG VQSNCLSVVP LETPYGRKRA
     IDQSSCNKDF SCAEGFCPSF VSVMGGSLKK SAAPKPDMDR LAARIAALPL PLVPELDAPY
     RLLVAGMGGT GVITIGALVS MAAHLQGLSA SVLDLTGLAQ KGGTVVSHLR LAPAHAAPGP
     VRLDWQQADA AILCDPLAAT APDSLGALAH GRTRVTVNTY VAPVSDFTRN PDAPLNAPAL
     LAKIEHAAGR EQTAAIDAHA AALALFGDSI LSNIFMLGYA WQRGDVPLSH AALDRAIELN
     GVAVASNRAA FNAGRLAAHE PEALAGMLAP KAQVIKLQVP ETLAQVVARR ESDLTAYQNA
     AYARAYREVV DAVAAREREL APEARSPRLA LAVARGLYKF MAYKDEYEVA RLYSDPAFQA
     QLDAQFEGDY TLRFHMAPPL LARKDPHTGV PRKMALGPRT RTVLRWLAHG KRLRGTWADP
     FGRTAERRTE RQLIDEYRAL VQRLLDGLTA DKIGEAATIA ALAESVRGYG HVKEAAIVRY
     REECARLLTS FETPGFVAIP VRRSA
//