ID A0A1S3BLY6_CUCME Unreviewed; 763 AA.
AC A0A1S3BLY6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=acetyl-CoA carboxytransferase {ECO:0000256|ARBA:ARBA00011883};
DE EC=2.1.3.15 {ECO:0000256|ARBA:ARBA00011883};
GN Name=LOC103490986 {ECO:0000313|RefSeq:XP_008448979.1,
GN ECO:0000313|RefSeq:XP_008448988.1, ECO:0000313|RefSeq:XP_008448996.1};
GN Synonyms=103490986 {ECO:0000313|EnsemblPlants:MELO3C003221.2.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008448996.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|EnsemblPlants:MELO3C003221.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008448979.1, ECO:0000313|RefSeq:XP_008448988.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001072};
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 RefSeq; XP_008448979.1; XM_008450757.2.
DR RefSeq; XP_008448988.1; XM_008450766.2.
DR RefSeq; XP_008448996.1; XM_008450774.2.
DR EnsemblPlants; MELO3C003221.2.1; MELO3C003221.2.1; MELO3C003221.2.
DR GeneID; 103490986; -.
DR Gramene; MELO3C003221.2.1; MELO3C003221.2.1; MELO3C003221.2.
DR KEGG; cmo:103490986; -.
DR eggNOG; ENOG502QPRP; Eukaryota.
DR OrthoDB; 331at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; Unplaced.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
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 HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR NCBIfam; TIGR00513; accA; 1.
DR NCBIfam; NF041504; AccA_sub; 1.
DR PANTHER; PTHR42853; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR42853:SF3; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679,
KW ECO:0000313|RefSeq:XP_008448979.1}.
FT DOMAIN 127..381
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 46..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 85352 MW; 870DC4844F9EF7FE CRC64;
MASISTPPAS FFSSSASDLL RSSSNGVSGL PLRALGRARF NPRRKDMSVS AKLRKGKKHE
YPWPDDADQN VKGGVLTHLS HFKPLKEKQK PVTLEFEKPL ILLEKKIIDV RKMAHETGLD
FSDQIISLEN KYQQALKDLY THLTPIQRVH IARHPNRPTF LDHVFNITEK FVELHGDRAG
YDDPAIVTGI GTIDGRRYMF MGHQKGRNTK ENIKRNFGMP TPHGYRKALR MMYYADHHGF
PIVTFVDTPG AFADLKSEEL GQGEAIAHNL RTMFGLKVPI ISIVIGEGGS GGALAIACAN
KLLMLENAVF YVASPEACAA ILWKDSKASP KAAEKLKITA TELTKLEIAD GIIPEPLGGA
HADPLWTSQQ IKLAINETMD ELLMMDTEKL LKHRMLKFRK IGGFQEGIPI EPERKFKMKK
KEEPIVGKIS VQELESKVEK VKQQILKAKE SSNAQSDVDL HEMIEHLEKE VDFEFSAAVK
AMGLKDRLAS LREEFLEANS SDQLIHPTLK EKIEKLRDEF NQGLSKAPNY ENLKNKLDML
KDLSRSKAHS VRDAKEASLK QEINKKFAEV LSRPDIQEKY EMLRAEIENL GASKYTDLDP
ELQNKMDKIK KEIQGELAAA LNSLGLDVEV LASKAQVLSE QSSLSLFKPK IEMLNEELSQ
GIESVIANRK DLKDMIELLK LEVAKAGKTP DATSKNRIGA LKQQIKERLA AALDSSDLKK
KHEKLREEIL ETAESGFDPT EGDSSVYGDA RIQTNSGAEH TFA
//
