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Database: UniProt
Entry: A0A2K6QXI4_RHIRO
LinkDB: A0A2K6QXI4_RHIRO
Original site: A0A2K6QXI4_RHIRO 
ID   A0A2K6QXI4_RHIRO        Unreviewed;      2442 AA.
AC   A0A2K6QXI4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN   Name=ACACB {ECO:0000313|Ensembl:ENSRROP00000033441.1};
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:ENSRROP00000033441.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000033441.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC         CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309;
CC         Evidence={ECO:0000256|ARBA:ARBA00001448};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR   STRING; 61622.ENSRROP00000033441; -.
DR   Ensembl; ENSRROT00000057879.1; ENSRROP00000033441.1; ENSRROG00000040293.1.
DR   GeneTree; ENSGT00940000155049; -.
DR   OMA; TEHCKVA; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0060421; P:positive regulation of heart growth; IEA:Ensembl.
DR   GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR049074; ACCA_BT.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45728:SF1; ACETYL-COA CARBOXYLASE 2; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF21385; ACCA_BT; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding 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; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200}.
FT   DOMAIN          243..745
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          402..593
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          872..946
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1679..2009
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          2013..2329
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2442 AA;  275600 MW;  371A4D17864FAB23 CRC64;
     FXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXPSMSGLHL VKRGREHKKL DLHRDFTVAS PAEFVTRFGG
     DRVIEKVLIA NNGIAAVKCM RSIRRWAYEM FRNERAIRFV VMVTPEDLKA NAEYIKMADQ
     YVPVPGGPNN NNYANVELIV DIAKRIPVQA VWAGWGHASE NPKLPELLCK NGVAFLGPPS
     EAMWALGDKI ASTIVAQTLQ VPTLPWSGSG LTVEWTEDDL QQGKIISVPE DVYDQGCVKD
     VDEGLEAAEK IGFPLMIKAS EGGGGKGIRK AESAEDFPIL FRQVQSEIPG SPIFLMKLAQ
     HARHLEVQIL ADQYGNAVSL FGRDCSIQRR HQKIVEEAPA TIAPLAIFEF MEQCAVRLAK
     TVGYVSAGTV EYLYSQDGSF HFLELNPRLQ VEHPCTEMIA DVNLPAAQLQ IAMGVPLHRL
     KDIRLLYGES PWGVTPISFE TPSNPPLARG HVIAARITSE NPDEGFKPSS GTVQELNFRS
     SKNVWGYFSV AATGGLHEFA DSQFGHCFSW GENREEAISN MVVALKELSI RGDFRTTVEY
     LINLLETESF QNNDIDTGWL DYLIAEKVQA EKPDIMLGVV CGALNVADAM FRTCMTDFLH
     SLERGQVLPA DSLLNIVDVE LIYGGIKYIL KVARQSLTMF VLIMNGCHIE IDAHRLNDGG
     LLLSYNGNSY TTYMKEEVDS YRITIGNKTC VFEKENDPTV LRSPSAGKLT QYTVEDGGHV
     EAGSSYAEME VMKMIMTLNV QESGRVKYIK RPGAVLEAGC VVARLELDDP SKVHPAEPFT
     GELPAQQTLP ILGEKLHQVF HSVLENLTNV MSGFCLPEPI FSIKLKEWVQ KLMMTLRHPS
     LPLLELQEIM TSVAGRIPAP VEKSVRRVMA QYASNITSVL CQFPSQQIAT ILDCHAATLQ
     RKADREVFFI NTQSIVQLVQ RYRSGIRGYM KTVVLDLLRR YLHVEHHFQQ AHYDKCVINL
     REQFKPDMSQ VLDCIFSHAQ VAKKNQLVIM LIDELCGPDP SLSDELTSIL NELTQLSKSE
     HCKVALRARQ ILIASHLPSY ELRHNQVESI FLSAIDMYGH QFCPENLKKL IISETTIFDV
     LPAFFYHANK VVCMASLEVY VRRGYIAYEL NSLQHRQLPD GTCVVEFQFM LPSSHPNRMT
     VPISITNPDL LRHSTELFMD SGFSPLCQRM GAMVAFRRFE DFTRNFDEVI SCFANVPKDT
     PLFSEARTSL YSEDDCKSLR EDPIHILNVS IQCADHLEDE ELVPILRTFV QSKKNILVDY
     GLRRITFLIA QEKEFPKFFT FRARDEFAED RIYRHLEPAL AFQLELSRMR NFDLTAVPCA
     NHKMHLYLGA AKVKEGAEVT DHRFFIRAII RHSDLITKEA SFEYLQNEGE RLLLEAMDEL
     EVAFNNTSVR TDCNHIFLNF VPTVIMDPLK IEESVRSMVM RYGSRLWKLR VLQAEVKINI
     HQTTTGSAVP IRLFITNESG YYLDISLYKE VTDSRSGNIM FHSFGNKQGP QHGMLINTPY
     VTKDLLQAKR FQAQSLGTTY IYDFPEIFRQ ALFKLWGSPD KYPKDILTYT ELVLDSQGQL
     VEMNRLPGGN EVGMVAFKMR FKTQEYPEGR DMIVIGNDIT FRIGSFGPGE DLLYLRASEM
     ARALGIPKIY VAANSGARIG MAEEIKHMFH VAWVDPEDPH KGFKYLYLTP QDYTRISSLN
     SVHCKHIEEG GESRYMITDI IGKDDGLGVE NLRGSGMIAG ESSLAYEEIV TISLVTCRAL
     GIGAYLVRLG QRVIQVENSH IILTGASALN KVLGREVYTS NNQLGGVQIM HYNGVSHITV
     PDDFEGVYTI LEWLSYMPKD NHSPVPIITP TDPIDREIEF LPSRAPYDPR WMLAGRPHPT
     LKGTWQSGFF DHGSFKEIMA PWAQTVVTGR ARLGGIPVGV IAVETRTVEV AVPADPANLD
     SEAKIIQQAG QVWFPDSAYK TAQAIKDFNR EKLPLMIFAN WRGFSGGMKD MYDQVLKFGA
     YIVDGLRQYK QPILIYIPPY AELRGGSWVV IDATINPLCI EMYADKESRG GVLEPEGTVE
     IKFRKKDLIK SMRRIDPAYK KLMEQLGEPD LSDKDRKDLE GRLKAREDLL LPIYHQVAVQ
     FADFHDTPGR MLEKGVISDI LEWKTARTFL YWRLRRLLLE DQVKQEILRA SGELSHVHIQ
     SMLRRWFVET EGAVKAYLWD NNQVVVQWLE QHWQVEDGPR STIRENITYL KHDSVLKTIR
     GLVQENPEVA VDCVIYLSQH ISPAERAQVI HLLSTMDSPA ST
//
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