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Database: UniProt
Entry: R5PRH1_9BACT
LinkDB: R5PRH1_9BACT
Original site: R5PRH1_9BACT 
ID   R5PRH1_9BACT            Unreviewed;       272 AA.
AC   R5PRH1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=2-oxoglutarate:acceptor oxidoreductase subunit OorB {ECO:0000313|EMBL:CCZ11512.1};
GN   ORFNames=BN465_00846 {ECO:0000313|EMBL:CCZ11512.1};
OS   Prevotella sp. CAG:1092.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ11512.1, ECO:0000313|Proteomes:UP000017987};
RN   [1] {ECO:0000313|EMBL:CCZ11512.1, ECO:0000313|Proteomes:UP000017987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987};
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:CCZ11512.1}.
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DR   EMBL; CAZL010000134; CCZ11512.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5PRH1; -.
DR   STRING; 1262919.BN465_00846; -.
DR   Proteomes; UP000017987; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017987}.
FT   DOMAIN          3..133
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   272 AA;  30015 MW;  F6983B1176D6321E CRC64;
     MQTIHGRAAA IATGAKVVNP NLTIWQISGD GDGLAIGGNH FIHAMRRNIN INMILLNNRI
     YGLTKGQYSP TSPRGFVSKS SPYGTVEDPF RPAELCFGAR GRFFARSVAT DGPETVEILK
     AAYHHKGAAV CEILQNCVIF NNGAYDAIYK KEGRQKNAIY VRHGEPLVFG ENNEYGLMQQ
     GFGLKVVKIG ENGVTINDIL VHDAHAEDDT LQLKLAMMDN EHGFPVALGV IRDVEAPTYD
     DAVNDQIAEV SKQKPYHCFE ELLETNDIWE VK
//
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