ID A0A1Q7TTR1_9CHLR Unreviewed; 463 AA.
AC A0A1Q7TTR1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:OLD91887.1};
GN ORFNames=AUG84_02980 {ECO:0000313|EMBL:OLD91887.1};
OS Chloroflexi bacterium 13_1_20CM_4_66_7.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805062 {ECO:0000313|EMBL:OLD91887.1, ECO:0000313|Proteomes:UP000187287};
RN [1] {ECO:0000313|EMBL:OLD91887.1, ECO:0000313|Proteomes:UP000187287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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:OLD91887.1}.
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DR EMBL; MNIW01000060; OLD91887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7TTR1; -.
DR Proteomes; UP000187287; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:OLD91887.1}.
FT DOMAIN 1..426
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 103..297
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 463 AA; 49510 MW; DD9E8FD145739DA6 CRC64;
MRACRELGIA TAAVYSDADR GAIHVRYADE AYHIGGAAAT ESYLQLDRIV QTAHDCGAEA
IHPGYGFLAE KPAFPEACDA AGLKFIGPPA SAMRALGSKL AARQLAAKNG VPVTPGTGAV
DPANARDEAR KIGFPVMLKP SGGGGGIGMK VVESEAQLEA AIESTAQAAR SAFGDATVYL
ERYALHPRHI EIQVICDSHG NAVHLGEREC SIQRRHQKIM EETPSPALTP EIRAAMGDAA
IRAARAAGYV NAGTVEFIFS DGNFYFLEVN ARLQVEHPIT EAVTGIDLVK EQIRVAAGLE
LSFAQSDIEW KGHAIEMRIN AEDPLRKFIP NPKRISRWVA PAGPGVRVDS GFGPGSDVPP
NYDSLVAKLI VHGTDRAEAI ARASRALREF VVVGPATTIP YHRAILDNPD FRAGNLSTRF
IEDHPQLVEQ ARKLAADQSP FDYGPDPRHV AAAAAAVASM VRR
//
