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Database: UniProt
Entry: A0A2K6NY27_RHIRO
LinkDB: A0A2K6NY27_RHIRO
Original site: A0A2K6NY27_RHIRO 
ID   A0A2K6NY27_RHIRO        Unreviewed;      1234 AA.
AC   A0A2K6NY27;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN   Name=PC {ECO:0000313|Ensembl:ENSRROP00000009184.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000009184.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000009184.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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DR   AlphaFoldDB; A0A2K6NY27; -.
DR   Ensembl; ENSRROT00000033267.1; ENSRROP00000009184.1; ENSRROG00000028920.1.
DR   GeneTree; ENSGT00900000141164; -.
DR   OrthoDB; 1129179at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 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   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   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; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200}.
FT   DOMAIN          92..542
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          212..409
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          619..888
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1165..1234
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1234 AA;  136186 MW;  FFCB5129CB9C9E66 CRC64;
     MEKLTKAPRA RSLRVRTQGC QDREPKLSPS YWMWLSSAGS RGVYCLPSGE LTKHLRMLKF
     RTVRGGLRLL GIRRTSTAPA ASPNVRRLEY KPIKKVMVAN RGEIAIRVFR ACTELGIRTV
     AIYSEQDTGQ MHRQKADEAY LIGRGLAPVQ AYLHIPDIIK VAKENNVDAV HPGYGFLSER
     ADFAQACQDA GVRFIGPSPE VVRKMGDKVE ARAIAIAAGV PVVPGTDAPI TSLHEAHEFS
     NTYGFPIIFK AAYGGGGRGM RVVHSYEELE ENYTRAYSEA LAAFGNGALF VEKFIEKPRH
     IEVQILGDQY GNILHLYERD CSIQRRHQKV VEIAPAAHLD PQLRTRLTSD SVKLAKQVGY
     ENAGTVEFLV DRHGKHYFIE VNSRLQVEHT VTEEITDVDL VHAQIHVAEG RSLPDLGLRQ
     ENIRINGCAI QCRVTTEDPA RSFQPDTGRI EVFRSGEGMG IRLDNASAFQ GAIISPHYDS
     LLVKVIAHGK DHPTAATKMS RALAEFRVRG VKTNIPFLQN VLNNQQFLAG TVDTQFIDEN
     PELFQLRPAQ NRAQKLLHYL GHVMVNGPTT PIPVKASPSP TDPIVPAVPI GPPPAGFRDI
     LLREGPEGFA RAVRNHQGLL LMDTTFRDAH QSLLATRVRT HDLKKIAPYV AHNFSKLFSM
     ENWGGATFDV AMRFLYECPW RRLQELRELI PNIPFQMLLR GANAVGYTNY PDNVVFKFCE
     VAKENGMDVF RVFDSLNYLP NMLLGMEAAG SAGGVVEAAI SYTGDVSDPS RTKYSLQYYM
     GLAEELVRAG THILCIKDMA GLLKPTACTM LVSSLRDRFP DLPLHIHTHD TSGAGVAAML
     ACAQAGADVV DVAADSMSGM TSQPSMGALV ACTRGTPLDT EVPMERVFDY SEYWEGARGL
     YAAFDCTATM KSGNSDVYEN EIPGGQYTNL HFQAHSMGLG SKFKEVKKAY VEANQMLGDL
     IKVTPSSKIV GDLAQFMVQN GLSRAEAEAQ AEELSFPRSV VEFLQGYIGV PHGGFPEPFR
     SKVLKDLPRV EGRPGASLPP LDLQALEKEL VDRHGEEVTP EDVLSAAMYP DVFAHFKDFT
     ATFGPLDSLN TRLFLQGPRI AEEFEVELER GKTLHIKALA VSDLNRAGQR QVFFELNGQL
     RSILVKDTQA MKEMHFHPKA LKDVKGQIGA PMPGKVIDIK VAAGAKVTKG QPLCVLSAMK
     METVVTSPME GTVRKVHVTK DMTLEGDDLI LEIE
//
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