ID A0A1J4U2F4_9BACT Unreviewed; 493 AA.
AC A0A1J4U2F4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:OIO17005.1};
GN ORFNames=AUJ54_10510 {ECO:0000313|EMBL:OIO17005.1};
OS Ignavibacteria bacterium CG1_02_37_35.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805220 {ECO:0000313|EMBL:OIO17005.1, ECO:0000313|Proteomes:UP000182308};
RN [1] {ECO:0000313|EMBL:OIO17005.1, ECO:0000313|Proteomes:UP000182308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_37_35 {ECO:0000313|EMBL:OIO17005.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO17005.1}.
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DR EMBL; MNVA01000150; OIO17005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4U2F4; -.
DR STRING; 1805220.AUJ54_10510; -.
DR Proteomes; UP000182308; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:OIO17005.1}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 493 AA; 55254 MW; 2009C9A321AFB413 CRC64;
MFKKILIANR GEIAVRIIRA CKELEIVSAS VYSESDKYAL HARLADESYF IGESLPSESY
LNQDKIIQLA KAINADAIHP GYGFLSENAS FIKKVEESGI VFIGPSSKSV EMMGSKTAAR
KLMKRNGVPI VPGTTEKILS LDAAKISANE IGYPILFKAS AGGGGKGMKR VFAETEIASA
FDSAQREALK AFGDDAVYIE KLVEHPKHIE VQIIADKFGN YCHLFERECS VQRRHQKVIE
EAPSSFLDEE TRKKLTSAAI NAAKSCGYFN AGTIEFLVDK YKNFFFLEMN TRLQVEHPVT
EFISGIDLVK EQMKIAAGEP LSFKQDDLHI LGHAIECRIY AEDPENNFLP ITGTVEYHRL
PSGPNIRVDR GIETGSEISR FYDPLLSKIS VMEKQRYAAI KRMDIALSDY LIAGIKTNIT
FLKRILKNDK FISGEYTIDL IEEDFSGVRE ICQNEDLENA AAIFSAYLKL LPQNNKHVKV
VSTSNKWTEL RYE
//
