ID   D6PCG4_9BACT            Unreviewed;       536 AA.
AC   D6PCG4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Pyruvate carboxylase {ECO:0008006|Google:ProtNLM};
OS   uncultured marine bacterium MedDCM-OCT-S04-C103.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=743049 {ECO:0000313|EMBL:ADD93415.1};
RN   [1] {ECO:0000313|EMBL:ADD93415.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20393571; DOI=10.1038/ismej.2010.44;
RA   Ghai R., Martin-Cuadrado A.B., Molto A.G., Heredia I.G., Cabrera R.,
RA   Martin J., Verdu M., Deschamps P., Moreira D., Lopez-Garcia P., Mira A.,
RA   Rodriguez-Valera F.;
RT   "Metagenome of the Mediterranean deep chlorophyll maximum studied by direct
RT   and fosmid library 454 pyrosequencing.";
RL   ISME J. 4:1154-1166(2010).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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DR   EMBL; GU942982; ADD93415.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6PCG4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 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; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432}.
FT   DOMAIN          1..192
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          458..536
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   536 AA;  58384 MW;  2DFFC39D0339DAB9 CRC64;
     MLLRGSNAVG YANYPDNVVR EFVIHSSEAG MDVFRIFDSL NYLPNLKVAM ETVAEKTHSL
     CEAAVCFTGD FTDSNEEKYV LKYYVELAKE LEKMGAHILA IKDMAGLCHP AAAQKLVKTL
     RNEISIPVHF HTHDSSGIAS ASVLKASEAG VDVVDLAVSS MSGCTSQPNL NSVAHALRNM
     PRSTGLDVDA LNELSLYWET IRQYYSPFDT SPPFGGAEVY QHQMPGGQYT NLREQATALG
     LGKRWPDVVK TYQEVNELLG DIVKVTPSSK CVGDLAIFLI TKGVKPSDLT NLPPETGFPE
     SVIDLMSGNL GQPTGGWPKD IQKVILGGRK PLRGRPGASA PKIDLAKESV KIKKKYGNKT
     TDDDLFSSLM YPKVYDDFRD FRNKYGDVSV LPTTAYFHGL KPGEEISIDI EEGKTLFIKL
     LHVGEPDEKG VRPLTFELNG KARTTLVKDQ SIKGDAKARE KADPANDMHI AAPIPAMISS
     IATSVGKNVA KGDKVAVLEA MKMQTTLYAS SKGVVDEILV GVGDSVESKD LVVRLR
//