ID Q5HQ53_STAEQ Unreviewed; 1147 AA.
AC Q5HQ53;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 114.
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 Name=pyc {ECO:0000313|EMBL:AAW54097.1};
GN OrderedLocusNames=SERP0704 {ECO:0000313|EMBL:AAW54097.1};
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW54097.1, ECO:0000313|Proteomes:UP000000531};
RN [1] {ECO:0000313|EMBL:AAW54097.1, ECO:0000313|Proteomes:UP000000531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531};
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J., Khouri H., Utterback T., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K., Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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};
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DR EMBL; CP000029; AAW54097.1; -; Genomic_DNA.
DR RefSeq; WP_002469569.1; NC_002976.3.
DR AlphaFoldDB; Q5HQ53; -.
DR STRING; 176279.SERP0704; -.
DR KEGG; ser:SERP0704; -.
DR eggNOG; COG1038; Bacteria.
DR HOGENOM; CLU_000395_0_1_9; -.
DR Proteomes; UP000000531; 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: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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
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; 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|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:AAW54097.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000531}.
FT DOMAIN 3..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 533..802
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 ACT_SITE 294
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 238
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 712
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 741
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 743
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 876
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 712
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; 128789 MW; EEE2C23F349A7A39 CRC64;
MKQIKKLLVA NRGEIAIRIF RAAAELNIST VAIYSNEDKS SLHRYKADES YLVGSDLGPA
ESYLNIERII EVALRAGVDA IHPGYGFLSE NEQFARRCAE EGIKFIGPHL EHLDMFGDKV
KARTTAINAN LPVIPGTDGP IESFEAAEQF ANEAGYPLMI KATSGGGGKG MRIVRESSEL
EDAFHRAKSE AEKSFGNSEV YIERYIDNPK HIEVQVIGDE FGNIIHLYER DCSVQRRHQK
VVEVAPSVGL SNKLRERICD AAIQLMENIK YVNAGTVEFL VSGDEFFFIE VNPRVQVEHT
ITEMITGIDI VKTQILVADG ESLFGDKISM PQQNEIQTLG YAIQCRITTE DPTNDFMPDS
GTIIAYRSSG GFGVRLDAGD GFQGAEISPY YDSLLVKLST HAVSFKQAEE KMERSLREMR
IRGVKTNIPF LINVMRNDKF RSGDYTTKFI EETPELFDIA PTLDRGTKTL EYIGNVTING
FPNVEKRPKP EYESTKIPKI SQKKINQLFG TKQILEQHGP TGVTNWVREQ EDVLITDTTF
RDAHQSLLAT RVRTKDMMNI ASKTAEVFKD SFSLEMWGGA TFDVAYNFLK ENPWERLERL
RKAIPNVLFQ MLLRASNAVG YKNYPDNVIK KFVHESAKAG VDVFRIFDSL NWVDQMKVAN
EAVQEAGMVS EGTICYTGDI LNAERSNIYT LDYYVKMAKE LEREGFHILA IKDMAGLLKP
KAAYELIGEL REATHLPIHL HTHDTSGNGL LTYKQAIDAG VDIIDTAVAS MSGLTSQPSA
NSLYYALNGF PRNLRTDIDG LEELSHYWSV VRPYYADFES DIKSPNTEIY QHEMPGGQYS
NLSQQAKSLG LGERFDEVKE MYRRVNFLFG DLVKVTPSSK VVGDMALYMV QNDLDEDTVI
NDGYKLDFPE SVVSFFKGDI GQPVNGFNKK LQDVILKGQQ PITERPGEYL EPVDFEAIRQ
ELSDIQQDEV TEQDIISYVL YPKVYKQYIQ TKEQFGNVSL LDTPTFLFGM RNGETVEIEI
DTGKRLIIKL ETISEPDENG KRTIYYAMNG QARRIYIQDE NVKTNANVKP KADKSNPNHI
GAQMPGSVTE VKVSVGDEVQ ANQPLLITEA MKMETTIQAP FDGIIKQINV ANGDAIATGD
LLVEIEK
//
