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Database: UniProt
Entry: A4AHX7_9ACTN
LinkDB: A4AHX7_9ACTN
Original site: A4AHX7_9ACTN 
ID   A4AHX7_9ACTN            Unreviewed;      1134 AA.
AC   A4AHX7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=A20C1_02056 {ECO:0000313|EMBL:EAR25333.1};
OS   marine actinobacterium PHSC20C1.
OC   Bacteria; Actinobacteria.
OX   NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR25333.1, ECO:0000313|Proteomes:UP000003868};
RN   [1] {ECO:0000313|EMBL:EAR25333.1, ECO:0000313|Proteomes:UP000003868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR25333.1,
RC   ECO:0000313|Proteomes:UP000003868};
RA   Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR25333.1}.
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DR   EMBL; AAOB01000004; EAR25333.1; -; Genomic_DNA.
DR   RefSeq; WP_009772060.1; NZ_CH672415.1.
DR   STRING; 312284.A20C1_02056; -.
DR   EnsemblBacteria; EAR25333; EAR25333; A20C1_02056.
DR   eggNOG; ENOG4108JIJ; Bacteria.
DR   eggNOG; COG1038; LUCA.
DR   OrthoDB; 361205at2; -.
DR   BioCyc; MACT312284:G1GNR-412-MONOMER; -.
DR   Proteomes; UP000003868; 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:UP000003868};
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:EAR25333.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003868}.
FT   DOMAIN        1    454       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      121    321       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      529    798       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1058   1132       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    296    296       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       538    538       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       708    708       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       737    737       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       739    739       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     117    117       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     200    200       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     235    235       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     610    610       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     872    872       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1134 AA;  122083 MW;  0447DA1B93C4EC65 CRC64;
     MFKKILVANR GEIAIRAMRA AVELGARTVA VFPYEDRNSV HRLKADEAYL IGEEGHPVRA
     YLDVSEIIRV AKECGADAIY PGYGFLSENP ELAHAAADAG IAFIGPPTKV LEMAGNKVTA
     KEHAIAAGVP VLKSTPASRD VDELLAGADD IGFPIFAKAV AGGGGRGMRR VEKKEDLRDA
     LVAAMREADS AFGDPTMFLE QAVVRPRHIE VQILADSHGN TIHLFERDCS VQRRHQKVVE
     IAPAPNLDEK TRQAMYSHAI AFAKSIDYVN AGTVEFLLDT AGERKGEHVF IEMNPRIQVE
     HTVTEEVTDV DLVQSQMRIA FGESLDELGL RQEELTLRGA ALQCRITTED PASGFRPDTG
     KITTYRSPGG AGIRLDGGTV SAGSQISPHF DSMLVKMTCR GRDFASAVRR ARRGLAEFRL
     RGVTTNIPFL QGVLDDPEFI AGDLSTAFID ERPELVNSHR SKDRGTKILT WLAEVTVNQP
     NGDGAGIINP QLKLPEVDLS IEAPAGSRQR LLELGPAGFA SALREQKALA VTETTFRDAH
     QSLLATRVRT RDLVAVMPHV ARLTPQLLSV EAWGGATYDV ALRFLAEDPW ERLASMREAL
     PNVAIQMLLR GRNTVGYTPY PTEVTDAFVR EAADTGVDIF RIFDALNDVS QMRPAIDAVL
     NTGTAVAEVA LCYTGDLLDP SEDLYTLDYY LKLADQIMES GAHVLAIKDM AGLLRAEAAE
     TLVAALRERF DAPVHVHTHD TAGGQLATLL AASRAGADAV DVASAPMAGT TSQPSMSALV
     ASLAHTARDT GISLDAVSNL EPYWEAVRHT YAPFESGLPG PTGRVYHHEI PGGQLSNLRQ
     QAIALGLADH FETIENLYAA ANKMLGRPPK VTPSSKVVGD LALALAAANA DPADFEENPD
     KYDIPDSVIG FMAGELGELP GGWPEPFRTK VLKGRNVKIG VEEVSKEDQA ALDGDPKDRR
     SALNRLLFAG PTQIFEKARE AYGDLSALAS TDYLYGLQQG HEHVVEIEKG VQLFVGLEAI
     GEADDKGMRT VMATLNGQLR PVFVRDLSIK VNSTAAEKAD ATKPGHVAAP FSGVVTLQVE
     EGAKVEAGQP VASIEAMKME AAITASVSGT VKRLAIPQTQ QVDAGDLLVE IEPS
//
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