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Database: UniProt
Entry: K6X9L3_9MICO
LinkDB: K6X9L3_9MICO
Original site: K6X9L3_9MICO 
ID   K6X9L3_9MICO            Unreviewed;      1147 AA.
AC   K6X9L3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   10-APR-2019, entry version 31.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   Name=pyc {ECO:0000313|EMBL:GAB95524.1};
GN   ORFNames=KILIM_022_00080 {ECO:0000313|EMBL:GAB95524.1};
OS   Kineosphaera limosa NBRC 100340.
OC   Bacteria; Actinobacteria; Micrococcales; Dermatophilaceae;
OC   Kineosphaera.
OX   NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB95524.1, ECO:0000313|Proteomes:UP000008366};
RN   [1] {ECO:0000313|EMBL:GAB95524.1, ECO:0000313|Proteomes:UP000008366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB95524.1,
RC   ECO:0000313|Proteomes:UP000008366};
RA   Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H.,
RA   Ando Y., Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step
CC       and the transfer of the carboxyl group to pyruvate in the second.
CC       {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=6.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAB95524.1}.
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DR   EMBL; BAHD01000022; GAB95524.1; -; Genomic_DNA.
DR   STRING; 1184609.KILIM_022_00080; -.
DR   EnsemblBacteria; GAB95524; GAB95524; KILIM_022_00080.
DR   Proteomes; UP000008366; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008366};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:GAB95524.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008366}.
FT   DOMAIN       20    469       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      140    336       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      544    813       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1067   1144       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    311    311       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       553    553       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       723    723       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       752    752       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       754    754       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     136    136       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     219    219       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     254    254       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     625    625       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     887    887       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1147 AA;  122658 MW;  9DFDC242A108CFBD CRC64;
     MATSASTETS PASTPSTPLG LRKILVANRG EIAIRAFRAA YELGAQSVAV FPYEDRGSEH
     RLKAEESYEI GERGHPVRAY LDPELIVRAA VKAGADAVYP GYGFLSENPE LAEACAREGL
     TFIGPGADVL SLTGDKSRAI AAAKAAGVPT LEGVAPTRDA DELVAAAQGL DYPLFVKAVA
     GGGGRGMRRV DEPEALREAV QACMREAEGA FGDPTVFVER AVVDPRHIEV QILADATGEV
     IHLFERDCSV QRRHQKVVEI APAPNLDPAI REAICADAVR FARHIGYVNA GTVEFLLDAA
     GQHHFIEMNP RIQVEHTVTE EVTDVDLVQS QMRIAGGATL ADLGLSQESV RLRGAALQCR
     ITTEDPANGF RPDTGKITTY RSPGGAGVRL DGGTTYAGAT ISPHFDSMLA KLTCRGADFP
     AAVARAARAV AEFRIRGVRT NIPFLQALLD DPDFRAGLLD TSFIERHPHL LTARSSADRG
     TRLLHYLADV SVNRPHGALP TAIEPRSKLP ELPEGTPVPD GSRQLLISHG PQGFARRLRE
     QKKVAVTDTT FRDAHQSLLA TRVRTYDLLG VAEHVAALTP QLFSLEAWGG ATYDVALRFL
     SEDPWERLAA LREAVPNICL QMLLRGRNTV GYTPYPTQVT DAFVAEAAAT GIDIFRIFDA
     LNDVEQMRPA IEAVRATDSA VAEVALCYTG DLSNPGERLY TLDYYLRLAE RIVEAGAHVL
     AIKDMAGLLR APAARTLVTA LRERFDLPVH LHTHDTAGGQ LATLTAAIDA GVDAVDAACA
     ALAGTTSQVA LSSLVAATDH SPRETGLSLE AVCALEPYWE AVRRVYAPFE SGLPAPTGRV
     YRHEIPGGQL SNLRQQAIAL GLGEKFEQIE DMYEAANRIL GNIVKVTPSS KVVGDLALHL
     VAVGADPAEF EADPARFDVP DSVIGFLSGE LGDPPGGWPE PFRTKALAGR TIKPAAADLD
     EEALHGLATD RRATLNRLLF PGPTRDFAES REKYGDVSVL PSTDFFYGLQ PGDEHEVRLQ
     EGKWLLLGLE AVGHADERGL RTAMCVINGQ LRPIVVQDRS IAAEVAETEK TDPSKPGHVA
     SPYDGAVTPT VAAGDQVEAG QAVATIEAMK MEASITAPVA GTVERLAIEG TGHLEGGDLV
     LVITPAQ
//
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