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Database: UniProt
Entry: A0A0T6AGA2_9BACT
LinkDB: A0A0T6AGA2_9BACT
Original site: A0A0T6AGA2_9BACT 
ID   A0A0T6AGA2_9BACT        Unreviewed;       482 AA.
AC   A0A0T6AGA2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   22-FEB-2023, entry version 13.
DE   SubName: Full=Pyruvate carboxylase subunit B, oxaloacetate decarboxylase, alpha subunit {ECO:0000313|EMBL:KRT74147.1};
DE            EC=4.1.1.3 {ECO:0000313|EMBL:KRT74147.1};
GN   ORFNames=XU13_C0009G0012 {ECO:0000313|EMBL:KRT74147.1};
OS   Candidatus Rokubacteria bacterium CSP1-6.
OC   Bacteria; Candidatus Rokubacteria.
OX   NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT74147.1, ECO:0000313|Proteomes:UP000051916};
RN   [1] {ECO:0000313|EMBL:KRT74147.1, ECO:0000313|Proteomes:UP000051916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT74147.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT74147.1}.
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DR   EMBL; LDXP01000009; KRT74147.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6AGA2; -.
DR   STRING; 1640509.XU13_C0009G0012; -.
DR   PATRIC; fig|1640509.3.peg.668; -.
DR   Proteomes; UP000051916; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:KRT74147.1};
KW   Pyruvate {ECO:0000313|EMBL:KRT74147.1}.
FT   DOMAIN          4..265
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   482 AA;  53613 MW;  8D7BDD497EF2E89C CRC64;
     MRKVSFIDTT LRDAHQSLWS TRMTTAMMLP VAPILDRLGF EAIDLVGGAV FDVCVRYLLE
     DPWERMRIMS RVITQTRLIV MTRGQSLFTF ELFPDDVVEL TAKRIAANGI RYTTPYDALN
     DIRNLEVPVR AAKAAGLYVA AGVVYTISPV HTDAYYTGKF RELLRLGVDA VFLKDPSGLL
     KPERVQTLIP VLRTAVGALP LQLHTHCLTG LGPICALEAI RLGVDTVHTA TSVLAHGASQ
     PPTEWVARNA RRLGFEVSLN VDGLQPVADH FRYIAAREGK PLGRVAEYDP FHYEHQIPGG
     MISNLRSQLR DIGLEHRLDE ILEESARVRR ELGYPIMVSP FSQFVATQAA LNVIQGERYA
     TVPDEIRKYA LGYYGQLPAP VDLDVLDRIV GREQPVTARP GELLAPALER VRRERGPFTS
     DDDLLLAVFY NPEQYLKLVN ARPIKTDYPI GRTPLATLIK ELAARGDIVS VKLIGKPPVP
     VA
//
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