ID A0A379MQY6_9BACT Unreviewed; 494 AA.
AC A0A379MQY6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=2-oxoglutarate carboxylase small subunit {ECO:0000313|EMBL:SUE33257.1};
DE EC=6.4.1.7 {ECO:0000313|EMBL:SUE33257.1};
GN Name=cfiB {ECO:0000313|EMBL:SUE33257.1};
GN ORFNames=NCTC11190_00461 {ECO:0000313|EMBL:SUE33257.1};
OS Rikenella microfusus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Rikenella.
OX NCBI_TaxID=28139 {ECO:0000313|EMBL:SUE33257.1, ECO:0000313|Proteomes:UP000255233};
RN [1] {ECO:0000313|EMBL:SUE33257.1, ECO:0000313|Proteomes:UP000255233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11190 {ECO:0000313|EMBL:SUE33257.1,
RC ECO:0000313|Proteomes:UP000255233};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UGVL01000001; SUE33257.1; -; Genomic_DNA.
DR RefSeq; WP_027290735.1; NZ_UGVL01000001.1.
DR AlphaFoldDB; A0A379MQY6; -.
DR STRING; 880526.GCA_000427365_00984; -.
DR GeneID; 78538817; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000255233; Unassembled WGS sequence.
DR GO; GO:0034029; F:2-oxoglutarate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SUE33257.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000255233}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 494 AA; 54790 MW; F29B7F5EC7EBDD3E CRC64;
MIKSILIANR GEIAIRICRT AKRMGIKTYV IRTTKEPNAV YLDFADKVID FPDTDGTVPE
FLDIDNLVKL AVENKVQAMH PGYGYLSENA DFAQKCTDAG IKFVGPPAKL IKDMGDKIIA
KEIAARNGVP MLQGSEGSVK DVKEGVKIAK KIGYPVIIKA ASGGGGRGMR IVHKQSEMEQ
MFHAASSEAQ SAFGDPSVFI EKYLENPKHI EFQVVADAHG NVVHLGEREC SVQRKHQKLL
EEAPSSGLDA ALRNKMARVA VKLAKGAGYE SLGTVEFLLD KNKNFYFMEM NTRIQVEHPI
TEAITGLDLV ELQLRIASGE KLPIRQSDVK LNGWAIECRI NAEDVQANFT PSMGVIKQLR
LPQGDNIRID TGIVPGSEIT PWFDSMIAKL IVHGKDRKQA IERMLSALER FHIKGVKTTI
PFCKAVLHNA AFCSGDFDTS FIETKLESLV YREPDEELMA AMLALYQYTH ETVPDVGPET
GIDPWVLNRR IRNL
//
