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Database: UniProt
Entry: R7JP37_9BACT
LinkDB: R7JP37_9BACT
Original site: R7JP37_9BACT 
ID   R7JP37_9BACT            Unreviewed;       615 AA.
AC   R7JP37;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=2-oxoacid:acceptor oxidoreductase alpha subunit {ECO:0000313|EMBL:CDE65421.1};
GN   ORFNames=BN752_01147 {ECO:0000313|EMBL:CDE65421.1};
OS   Alistipes putredinis CAG:67.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1263036 {ECO:0000313|EMBL:CDE65421.1, ECO:0000313|Proteomes:UP000018026};
RN   [1] {ECO:0000313|EMBL:CDE65421.1, ECO:0000313|Proteomes:UP000018026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:67 {ECO:0000313|Proteomes:UP000018026};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDE65421.1}.
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DR   EMBL; CBJI010000094; CDE65421.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7JP37; -.
DR   Proteomes; UP000018026; 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; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
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; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03710; OAFO_sf; 1.
DR   PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018026}.
FT   DOMAIN          21..212
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          261..470
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          515..605
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   615 AA;  66848 MW;  899C4842C8E08E0B CRC64;
     MNENKVQELQ DVVIRFSGDS GDGMQLTGTL FSDTSALLGN GISTFPDYPA EIRAPQGTVA
     GVSGFQVHFG AKRQLNPGDF CDVLIAMNPA ALKANRKWLK PGATVILDED SITEEHLRKA
     GFATLDPIRE LNLEDFNVVV PNITEMTKAA LADSGLDNKA MVKCKNMFAL GICFYLYNRP
     EDHAKRYLDS KFAKKNPAIA EANKRAIDAG YNYAANTHQF ANTYTVASGQ MEKGTYRSIS
     GNVATAWGLC AASEKSGLPL FCGSYPITPA TVILEELAKR KDLGVKTVQA EDEIAGICTA
     IGASFAGNFA VTTTSGPGLS LKSEALGLAV MTELPLVVVD VQRGGPSTGL PTKTEQSDLQ
     QALYGRNGES PVAVIAASMP SDCFHYAFEA GRIAMEHMTP VVLLSDGFIA NGSEPWKIPS
     MKDYPTINPP IIDKTEDGGP FMPYARNEKL ARSWAFPGKA GLEHRVGGLE KDKLKGSIST
     DAQNHQEMTN LRAAKIAKIA DYIPHQTVYG DPEGDLLVVG WGGTRGHLQN AVDKMRAEGK
     KVSLCHFNYI NPLPHGVADI FKRFKKIVVC ELNEGQFANY LRGKLQQFDY EQYNKCEGQP
     FTVTELTNKF HSLLK
//
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