ID A0A2R8AZI0_9RHOB Unreviewed; 339 AA.
AC A0A2R8AZI0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=2-oxoglutarate carboxylase large subunit {ECO:0000313|EMBL:SPF81455.1};
DE EC=6.4.1.7 {ECO:0000313|EMBL:SPF81455.1};
GN Name=cfiA_2 {ECO:0000313|EMBL:SPF81455.1};
GN ORFNames=PRI8871_03278 {ECO:0000313|EMBL:SPF81455.1};
OS Pseudoprimorskyibacter insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudoprimorskyibacter.
OX NCBI_TaxID=1695997 {ECO:0000313|EMBL:SPF81455.1, ECO:0000313|Proteomes:UP000244904};
RN [1] {ECO:0000313|Proteomes:UP000244904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8871 {ECO:0000313|Proteomes:UP000244904};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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DR EMBL; OMOJ01000010; SPF81455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AZI0; -.
DR Proteomes; UP000244904; Unassembled WGS sequence.
DR GO; GO:0034029; F:2-oxoglutarate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Ligase {ECO:0000313|EMBL:SPF81455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244904}.
FT DOMAIN 262..337
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 339 AA; 36867 MW; 5D8C066FBCF890E4 CRC64;
MRGQYAAFES SLQAPASEVY LHEMPGGQFT NLKAQARSMG LEERWHEVAQ AYADVNMMFG
DIVKVTPSSK VVGDMALMMV SQNLTRSEVE DPKVDVSFPD SVIDMMKGNL GQPPGGWPKA
IQSKIMKGDK AFTVRPGSLA APVDIEDTRA ELSEKLDGLA VDDEDLNGYL MYPKVFLDYI
GRHRDYGPVR TLPTPVFFYG MEPGDEISAE IDPGKKLEIR LQAVGETDEA GDVKVFFELN
GQPRTVRVPN RMVKSATAAR PKAQTGNADH IGAPMPGVVA SVAVQVGQQV HKGDLLLTIE
AMKMETGLSA DRDATVKSIH VTHGAQIEAK DLLIELEGP
//
