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Database: UniProt
Entry: R6Y3D8_9BACT
LinkDB: R6Y3D8_9BACT
Original site: R6Y3D8_9BACT 
ID   R6Y3D8_9BACT            Unreviewed;       617 AA.
AC   R6Y3D8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Pyruvate/oxaloacetate carboxyltransferase {ECO:0000313|EMBL:CDD25834.1};
GN   ORFNames=BN590_00053 {ECO:0000313|EMBL:CDD25834.1};
OS   Alistipes sp. CAG:29.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1262694 {ECO:0000313|EMBL:CDD25834.1, ECO:0000313|Proteomes:UP000018138};
RN   [1] {ECO:0000313|EMBL:CDD25834.1, ECO:0000313|Proteomes:UP000018138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:29 {ECO:0000313|Proteomes:UP000018138};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDD25834.1}.
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DR   EMBL; CBGS010000181; CDD25834.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6Y3D8; -.
DR   Proteomes; UP000018138; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 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   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:CDD25834.1};
KW   Transferase {ECO:0000313|EMBL:CDD25834.1}.
FT   DOMAIN          5..285
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          541..617
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   617 AA;  67411 MW;  BBD284B39FEE9E62 CRC64;
     MARNLKIRDL TLRDGQQSSF ATRMSQAQVD RCLPFYKDAN FYAMEVWGGA VPDSVMRYLN
     ENPWTRLETI YKAVGKVSKL TALSRGRNLF GYAPYPDDVI DGFCRNAIES GLGIMRIFDA
     LNDVDNVKST IKYVKQYGGI ADCAVCYTVD PKYPEPSFMQ RLMGKKQPQP VFTDAYFLDK
     AKQMAALGAD MITIKDMSGL IPPRRVATLV KLFKKNISIP VDFHTHCTPG YGLASVLAAI
     VAGVDIVDTN CWYFAEGTGA PAIELVHVFC KKLGVDTGVN MEAVAKINTQ LREIRKELNQ
     SVFGADKPEP KAFNPLTDKL PAEIDALFDK AIAAAKADDE DATIDACRKI EAYFGFPAPN
     ELVQKAEIPG GMYSNMVAQL KQLKAEDILP RAMELIPSVR LAAGLPPLVT PTSQIVGAQA
     VNCALDEKAG RPMYTNKSSQ FVGLVKGEYG HTPVKIDPEF RFKICGVREE TPYDTSKYQM
     QPNPELPEAG GVKLAANGKE VLLLELFPMV AKTFLTDMKV KAYAAAKPAE PKAEEKKVEE
     VKKIVITGNA VTAPLPGRII ELKVKVGDTV KAGDEIAVLE AMKMENSVTT DYAGTVKQVL
     VQPGENVATD AVLAEIG
//
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