ID G2FI96_9GAMM Unreviewed; 317 AA.
AC G2FI96;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=2-oxoglutarate oxidoreductase, beta subunit {ECO:0000313|EMBL:EGW53449.1};
DE EC=1.2.7.3 {ECO:0000313|EMBL:EGW53449.1};
GN Name=oorB3 {ECO:0000313|EMBL:EGW53449.1};
GN ORFNames=TevJSym_bb00040 {ECO:0000313|EMBL:EGW53449.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53449.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW53449.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW53449.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFZB01000028; EGW53449.1; -; Genomic_DNA.
DR RefSeq; WP_005958509.1; NZ_AFZB01000028.1.
DR AlphaFoldDB; G2FI96; -.
DR PATRIC; fig|1049564.3.peg.2632; -.
DR eggNOG; COG1013; Bacteria.
DR Proteomes; UP000005167; Unassembled WGS sequence.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03375; TPP_OGFOR; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR032686; PFO_beta_C.
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; PF12367; PFO_beta_C; 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 ECO:0000313|EMBL:EGW53449.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167}.
FT DOMAIN 62..209
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 252..292
FT /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12367"
FT REGION 142..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 35074 MW; 44E48D1A31E1AE4B CRC64;
MFGLKADWSL EVFERYFTLG DYAGGEARWC PGCGDFAVLN ATHRVLRDAQ MPPEKSVFVS
GIGCSSRMPH YVGTYGFHGL HGRALPIANG VKSRRPDLDV WVATGDGDCF SIGAGPWIHA
MRLNMDMVVL IFDNGIYGLT KKQTSPTTPT GMKTNTHPRG ALLPPLNPLT TTLSISNVSF
VAQVPDWNPP MLYETIKAAH QHRGTSFVRI LQRCPVFSDE FCKPMQENPE QMLVLTHENG
IPMDDSVLRV FKETQEHDPA DWLGAMALAH DTTRIPLGLL YRNPDAVVYE DLSAQGLEKT
NEEKLAAIDK AIDAFSI
//