GenomeNet

Database: UniProt
Entry: G2FI96_9GAMM
LinkDB: G2FI96_9GAMM
Original site: G2FI96_9GAMM 
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
//
DBGET integrated database retrieval system