ID A0A8D2LWN5_VARKO Unreviewed; 2337 AA.
AC A0A8D2LWN5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
OS Varanus komodoensis (Komodo dragon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX NCBI_TaxID=61221 {ECO:0000313|Ensembl:ENSVKKP00000028136.1, ECO:0000313|Proteomes:UP000694545};
RN [1] {ECO:0000313|Ensembl:ENSVKKP00000028136.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSVKKP00000028136.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSVKKT00000028812.1; ENSVKKP00000028136.1; ENSVKKG00000018225.1.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000694545; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
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: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:000005; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 3.90.1770.10:FF:000001; acetyl-CoA carboxylase 1; 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; 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; IPR001882; Biotin_BS.
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:SF5; ACETYL-COA CARBOXYLASE 1; 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; PS00188; BIOTIN; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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 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:UP000694545};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2337
FT /note="acetyl-CoA carboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034330955"
FT DOMAIN 143..644
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 301..492
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 771..845
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1566..1904
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1908..2224
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2337 AA; 263341 MW; 2780A226D797FF72 CRC64;
TQTGWWGGAL EWSLLEKGLA AYLGGTMGDP APVDKPLELS VHSRFIIGSV SEDNSEDETS
SLVKIDLLED KEQSLSPVSV SSDSLSDLVP SNVQDGLAVH MRPSMSGLHL MKQGRDRKKV
ELQRDFTVAS PAEFVTRFGG TKVIEKVLIA NNGIAAVKCM RSIRRWSYEM FRNERAIRFV
VMVTPEDLKA NAEYIKMADH YVPVPGGPNN NNYANVELIL DIAKRIPVQA VWAGWGHASE
NPKLPELLHK NGIAFMGPPS QAMWALGDKI ASSIVAQTAG IPTLPWSGSG LQVHWQENEF
QKRILSVPQE LYEKGCVTDV DDGLRAAEEV GYPVMIKASE GGGGKGIRKV NNAEDFPNLF
RQVQAEVPGS PIFVMRLAKQ SRHLEVQILA DQYGNAISLF GRDCSVQRRH QKIIEEAPAS
IATLAVFEHM EQCAVKLAKM VGYVSAGTVE YLYSQDGSFY FLELNPRLQV EHPCTEMVAD
VNLPSAQLQI AMGIPLHRIK DIRVMYGASP WGDSPIDFEN SAHVPCPRGH VIAARITSEN
PDEGFKPSSG TVQELNFRSN KNVWGYFSVA AAGGLHEFAD SQFGHCFSWG ENREEAISNM
VVALKELSIR GDFRTTVEYL IKLLETESFQ QNRIDTGWLD RLIAEKVQAE RPDTMLGVVC
GALHVADVSF RNSVSNFLHS LERGQVLPAH TLLNTVDVEL IYEGRKYVLK VTRQSPNSYV
VIMSGSCVEV DVHRLSDGGL LLSYDGSSYT TYMKEEVDRY RITIGNKTCV FEKENDPSIL
RSPSAGKLIQ YVVEDGGHVF AGQCFAEIEV MKMVMTLTAA ESGCIHYVKR PGAALDPGCV
IAKLQLDDPS RVQQAELHTG ALPKIQSTAL RGEKLHRVFH YVLDNLVNVM NGYCLPEPFF
NSKVKDWVER LMKTLRDPSL PLLELQDIMT SVSGRIPPNV EKSIKKEMAQ YASNITSVLC
QFPSQQIANI LDSHAATLNR KSEREVFFMN TQSIVQLVQR YRSGIRGHMK AVVMDLLRQY
LKVETQFQHG HYDKCVFALR EENKSDMNTV LNYIFSHAQV TKKNLLVTML IDQLCGRDPT
LTDELINILT ELTQLSKTTN AKVALRARQV LIASHLPSYE LRHNQVESIF LSAIDMYGHQ
FCIENLQKLI LSETSIFDVL PNFFYHSNQV VRMAALEVYV RRAYIAYELN SVQHRQLKDN
TCVVEFQFML PTSHPNRMSF SSNLNHYGMV HVASVSDVLL DNSFTPPCQR MGAMVSFRTF
DEFVRLFDEV MGCFCDSPPQ SPTFPEAGHP SLYDEDKVPA RDEPIHILNI AIKTDCDIDD
EGLAAMFREF TQSKKSVLID HGIRRLTFLV AQKFEEDRIY RHLEPALAFQ LELNRMRNFD
LTAIPCANHK MHLYLGAAKV EAGAEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL
LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG SRLWKLRVLQ
AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD PRTAQIMFQA YGDKQGPLHG
MLINTPYVTK DLLQSKRFQA QSLGTTYVYD IPEMFRQSLI KLWDSMKELA TLPAPPLPSD
MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWLMTLKSPE YPDGRDIIVI SNDITYRIGS
FGPQEDLLYL RASELARLQG IPRIYVAANS GARIGLAEEI RHMFHVAWED PADPYKGFKY
LYLTPQDYKK VSALNSVHCE HVEDGGESRY KITDVIGKEE GIGTENLRGS GMIAGESSLA
YEEIITINLV TCRAIGIGAY IVRLGQRTIQ VENSHIILTG AGALNKVLGR EVYTSNNQLG
GIQIMHNNGV THKTVCDDFE GVYSILQWLS YMPKSVSSPV PVLPVKDPID RAIDFVPTKT
PYDPRWMLAG RPHPTQKGQW LSGFFDHSSF LEIMQPWAQT VVVGRARLGG IPVGVVAVET
RTVELSIPAD PANLDSEAKV IQQAGQVWFP DSAFKTAQAI KDFNREGLPL MVFANWRGFS
GGMKDMYDQV LKFGAYIVDG LREYKQPVLV YIPPQAELRG GSWVVIDSTI NPRHMEMYAD
RESRGGILEP EGTVEIKFRK KDLVKTMRRV DPVYVQLAER LGTPELSQAE RKELETKLKE
REEFLIPIYH QVAVQFADLH DTPGRMQEKG VITDILDWKT SRTFFYWRLR RLLLEDLVKK
KIHGANPELT DGQIQAMLRR WFVEVEGTVK AYLWDNNRDL VEWLEKQLAE DEGARSVVDE
NIKYISRDYV LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEIVRILST MDAPAST
//
