ID A0A835PE32_VANPL Unreviewed; 2172 AA.
AC A0A835PE32;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Acetyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HPP92_027255 {ECO:0000313|EMBL:KAG0449808.1};
OS Vanilla planifolia (Vanilla).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Vanilloideae; Vanilleae; Vanilla.
OX NCBI_TaxID=51239 {ECO:0000313|EMBL:KAG0449808.1, ECO:0000313|Proteomes:UP000636800};
RN [1] {ECO:0000313|EMBL:KAG0449808.1, ECO:0000313|Proteomes:UP000636800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG0449808.1};
RA Hasing T., Tang H., Brym M., Khazi F., Huang T., Chambers A.H.;
RT "A phased Vanilla planifolia genome enables genetic improvement of flavour
RT and production.";
RL Nat. Food 1:811-819(2020).
CC -!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation of
CC acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty
CC acid synthesis and in the cytosol in various biosynthetic pathways
CC including fatty acid elongation. {ECO:0000256|ARBA:ARBA00057508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP =
CC N(6)-carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H(+);
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00048600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP +
CC phosphate + H(+); 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:ARBA00048065};
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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG0449808.1}.
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DR EMBL; JADCNL010000161; KAG0449808.1; -; Genomic_DNA.
DR OrthoDB; 423427at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000636800; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd06850; biotinyl_domain; 1.
DR FunFam; 2.40.460.10:FF:000001; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 2.40.50.100:FF:000005; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 3.30.470.20:FF:000043; acetyl-CoA carboxylase 1-like; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.40.50.20:FF:000005; acetyl-CoA carboxylase isoform X2; 1.
DR FunFam; 3.90.226.10:FF:000010; acetyl-CoA carboxylase isoform X2; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 2.
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; 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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 2.
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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000636800}.
FT DOMAIN 38..545
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 191..385
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 633..707
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1413..1753
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1757..2073
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2172 AA; 241552 MW; 0DD34C3619E839EC CRC64;
MAESWHLNGG VHGMSPVKDA SLIAEVDQFC YALGGKTPIH SILIANNGMA AVKFMRSIRT
WAYETFGSEK AILLVAMATP EDLRINAEHI RIADQFVEVP GGTNNNNYAN VQLIVEKAEM
THVSAVWPGW GHASENPELP DALKAKGIIF LGPPAAPMAA LGDKIGSSLI AQAAGVPTLP
WSGSNVKISE GNCLESIPDD IYHQACVYTT EEALASCQVV GYPAMIKASW GGGGKGIRKV
HNDEEVKALF KQVQGEVPGS PIFIMKVASQ SRHLEVQLLC DEYGNVAALH SRDCSVQRRH
QKIIEEGPIT IAPLETIKQL EQAARRLAKC VNYVGAATVE YLFSMETGEY YFLELNPRLQ
VEHPVTEWIA EVNLPAAQVA VGMGIPLWQI PEIRRFYGKD HSGGYDAWRK TSIAATPFDF
DKAESIKPKG HCVAVRVTSE DPDDGFKPTS GKVQELVFKS KPNVWAYFSV KSGGGIHEFS
DSQFGHVFAF GESRALAIAN MILGLKEVQI RGEIRTNVDY TIDLLNSSEY KDNKVHTGWL
DSRIAMRVRA ERPPWYLSVV GGALYKASTS SATIVSDYVG YLVKGQIPPK HISLVNSTVS
LNIEGSKYTI EMLNGNSHVI YAEEEAAGTA FLLMNEHDPS RLVAETPCKL LRYLVPDSEH
LDADTPYAEV EVMKMCMPLL LPASGVIHFV MSEGQAMQAG DLIARLDLDD PSAVKRAEPF
HGTFPKLGLP TAVSDKVHQR CAASLNAARM ILAGYEHNIT QVVQDLLNCL DNPELPFLQW
QESMSVLATR LPKDLKNELD SKYKVYEMRT TYQKNVEFPA KLLKGIFEAH LSSLPEKEKA
TQERLLEPLI SLVTSYEGGR ESHARVIVQS LFEEYLFVEE LFSDAIQGVR SKNKLILRLM
EALVYPNPAA YRDQLIRFSS LNHMAYSEVW NLVAASLRGT HLYAEEKTAI NERMEDLVSV
PLAVEDALVS LFDHSDPTLQ RRVVETYIRR LYQPYLVKGS IRMQWHRAGL IALWEFSEEH
IQKRNGSVDT MAEKPLLEKH CEKKWGAMVI IKSLQFLPAA INAALKESAN SLNPKGDNEL
LSNDLPEKAI QGNMLHVALV GINNQMSALQ DSGDEDQAQE RIDKIAKILK EDIISADLSG
AGIRVISCII QRDEGRAPMR HSFHWSSDKL YFEEEPQLRH LEPPLSTFLE LDKLKGYKNV
RYTPSRDRQW HLFSVLDGNV PIPRMFLRTI VRQPNTAEGF SSHHALDIDS SHARHSMSFT
SISILRCILT ALEELELNVH NATIRSEHSH MYLCILREQQ LYDLVPHSRT LDASADQEDS
LICSILEELA LAVHESVGVR MHRLAVCEWE VKLLLATDGV ACGAWRIVVT NVTGHTCTVH
VYRELDDSRT HEVVYHSASL VPGPLDGVPL SAWYQPLSAI DRRRLSARRN NTTYCYDFPL
AFETALWRSW TSNCFNDKKG IGCKDVLKVT ELVFADKNWN WDTALVPVDR SPGLNDVGII
AWSMEMLTPE FPGGRKIIVV ANDVTHQAGS FGPKEDAFFY AVSNLACKLK LPLIYLAANS
GARIGAAEEV RSCFRVAWSD ESNPERGFQY IYLTPEDYSR IQSSVIAHEL KLQSGETRWV
IDTIVGKQDG LGVENLAGSG AIASAYSKAY KETFTLTFVT GRTVGIGAYL ARLGMRCIQR
LDHPIILTGF SALNKLLGRE VYSSHMQLGG PKIMATNGVV HLTVPDDLEG VSAILKWLSY
VPPFVGGPLP ISRSLDPPER AVEYIPENSC DPRAAISGLK DSSGKWLGGI FDKDSFVETL
EGWAKTVVTG RAKLGGIPVG VIAVETQTVM QVIPADPGQL DSHERVVPQA GQVWFPDSAA
KTAQALMDFN REELPLFILA NWRGFSGGQR DLFEGILQAG STIVENLRTY KQPAFVYIPM
MGERRGGAWV VVDSNINPDQ IEMYAERTAK GNVLEPEGMI EIKFRPKEIV DCMGRLDHEL
INLKAKLQEA KVGRLSHELV DSLQKTITER EKKLLPTYAQ IATKFAELHD TSLRMAAKGV
VREVVDWKSS RTFFYNRLNR RVSEWSLIKS AKEASGEELS DKSALELIKN WFLASGAEWV
DDEAFFAWKD DAHGCQTHLK ELRAKRVLSQ LSRLGESASD LDALRQGLAA LLSRVDPSSR
GKLIEDFTKL AE
//
