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Database: UniProt
Entry: A1WU33_HALHL
LinkDB: A1WU33_HALHL
Original site: A1WU33_HALHL 
ID   A1WU33_HALHL            Unreviewed;      1147 AA.
AC   A1WU33;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN   OrderedLocusNames=Hhal_0402 {ECO:0000313|EMBL:ABM61195.1};
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM61195.1, ECO:0000313|Proteomes:UP000000647};
RN   [1] {ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABM61195.1, ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX   PubMed=23991253; DOI=10.4056/sigs.3677284;
RA   Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA   Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA   Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA   Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT   "Complete genome sequence of Halorhodospira halophila SL1.";
RL   Stand. Genomic Sci. 8:206-214(2013).
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step and
CC       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(+) + oxaloacetate
CC         + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, 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|ARBA:ARBA00001953,
CC         ECO:0000256|PIRNR:PIRNR001594};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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DR   EMBL; CP000544; ABM61195.1; -; Genomic_DNA.
DR   RefSeq; WP_011813218.1; NC_008789.1.
DR   AlphaFoldDB; A1WU33; -.
DR   STRING; 349124.Hhal_0402; -.
DR   KEGG; hha:Hhal_0402; -.
DR   eggNOG; COG1038; Bacteria.
DR   HOGENOM; CLU_000395_0_1_6; -.
DR   OMA; YAIQSRV; -.
DR   OrthoDB; 9760256at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000647; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniPathway.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 2.
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   NCBIfam; TIGR01235; pyruv_carbox; 1.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
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; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:ABM61195.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000647}.
FT   DOMAIN          3..456
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          123..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          533..801
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1071..1146
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          482..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..507
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         542
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         614
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         711
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         740
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         742
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         875
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         711
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1112
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1147 AA;  126104 MW;  6CCD53684CDB1B94 CRC64;
     MVPFQKILIA NRGEIAIRVM RAANELGKRT VAIYAQEDKL GLHRFKADEA YQVGEGMGPV
     EAYLSIDEVI RVAKMAGADA VHPGYGLLSE NPELVDACEA AGITFIGPRA DTMRALGDKA
     SARRVAIEAG VPVIPASEVL GDDIEAARRW ADEIGYPMML KASWGGGGRG MRPIREPEEL
     EARVLEGRRE AEAAFGSGEG YLEKMIERAR HVEVQVLGDT HGGLYHLFER DCTVQRRNQK
     VVERAPAPYL TEAQRAEVCD LGLKVARHVG YQNAGTVEFL MDMDTDTFYF IEVNPRIQVE
     HTVTEEVTGI DIVKAQIRIA EGEHLAAATG KADQGALWLN GHAMQCRVTT EDPQNNFIPD
     YGRITAYRSA TGMGIRLDGG TAYAGGVITR YYDSLLVKVT AWAPTPQEAI SRMDRALREF
     RIRGVSTNIP FVENLLKHPA FLDNSYTTRF IDTAPELFDF DKRRDRATRL LTYLAEITVN
     GHPETLGRPQ PAAGLPLPVP PEPRDEPAPG TRNLLEAQGP QAVADWLAGR KELLLTDTTM
     RDAHQSLLAT RMRSFDMARV APAYAANLPQ LFSVECWGGA TFDVAYRFLQ ECPWQRLRQI
     REAMPNVMTQ MLLRGSNGVG YTNYPDNVVR AFVHQAADSG VDVFRVFDSL NWVENMRVAM
     DAVLESGKVC EGTLCYTGDI LDPGRDKYDL KYYVAMGKAL RDAGAHILGV KDMAGLLKPA
     AARVLFRALK EEVGLPIHFH THDTSGIAGA TVLAAADAGV DVADVAMDAF SGNTSQPVFG
     SIVEALRHTE RDTGLDMSAV REISNYWEQV RAHYAAFETG QQSPSSEVYL HEMPGGQFTN
     LKAQARSLGL EERWHEVAQA YADANQIFGD IVKVTPSSKV VGDMALMMVS QGLTREQVED
     PAVDVNFPDS VIDMLRGNLG HPPGGWPEGI QKKALKGEQP LQDRPGKYLE PLDLEAVRQQ
     ASDELDGAEI DDEDLNGYLM YPKVFTEYKR RRERFGPVRT LPTRNFFYGM EAGEEISVDI
     DPGKTLEIRL MTVSEPGEDG DRRVFFELNG QPRTVRVADN QAKAQVVQTP KAEEGNPAHV
     GAPTPGVVAS VAATPGQNVK AGDVLLIIEA MKMEMGLHAE RDGVVKAVHV QPGSQIEAKD
     LLVEFEA
//
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