UniProt: A0A670JFX1

Database: UniProt
Entry: A0A670JFX1_PODMU

LinkDB:  A0A670JFX1_PODMU 
Original site:  A0A670JFX1_PODMU

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (32)   
   InterPro (17)   
   Pfam (7)   
   PROSITE (7)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (43)   

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ID   A0A670JFX1_PODMU        Unreviewed;      2212 AA.
AC   A0A670JFX1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 26.
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:ENSPMRP00000023528.1};
OS   Podarcis muralis (Wall lizard) (Lacerta muralis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC   Lacertibaenia; Lacertidae; Podarcis.
OX   NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000023528.1, ECO:0000313|Proteomes:UP000472272};
RN   [1] {ECO:0000313|Ensembl:ENSPMRP00000023528.1, ECO:0000313|Proteomes:UP000472272}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA   Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA   Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA   Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA   Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA   Andersson L., Carneiro M.;
RT   "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT   polymorphisms in the wall lizard.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN   [2] {ECO:0000313|Ensembl:ENSPMRP00000023528.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSPMRP00000023528.1}
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}.
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DR   Ensembl; ENSPMRT00000024971.1; ENSPMRP00000023528.1; ENSPMRG00000013605.1.
DR   GeneTree; ENSGT00940000155049; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000472272; Chromosome 13.
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: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   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; 3.30.1490.20: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; 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:SF1; ACETYL-COA CARBOXYLASE 2; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 2.
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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000472272}.
FT   DOMAIN          113..615
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          270..463
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          742..816
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1523..1853
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1857..2130
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2212 AA;  249960 MW;  4CE4D851EFB03CF1 CRC64;
     QLSNDHFGLK RGEKQQQEMW NYSVQEWWFE SLLLLELPFW FQGVAACDSC FLSVLPGQPP
     LFISLRLLTP SRPSMSGMHL TKKGREQRKL DLHRDFTVAS PAEFVTRFGG NRVIEKVLIA
     NNGIAAVKCM RSIRRWAYEM FRNERAIRFV VMVTPEDLKA NAEYIKMADQ YVPVPGGTNN
     NNYANVELIV DISKRIPVQA VWAGWGHASE NPKLPELLHK HGIAFLGPPS EAMWALGDKV
     ASTIVAQTVH IPTLPWSGSG LVAEWMEDEK EQPRTITVPL ETYWQGCVRD QDEGLEASER
     IGYPVMIKAS EGGGGKGIRI VEAAEEFPTR FRQVQSEAPG SPIFVMKLLQ HARHLEVQVL
     ADQYGNAVSL FSRDCSIQRR HQKIIEEAPA TVAATSVFEY MEQCAVRLAK IVGYVSAGTV
     EYLYSEDGSF HFLELNPRLQ VEHPCTEMIA DVNLPAAQLQ IAMGVPLHRL KDIRALYGEP
     PWGDSPIAFE SPSNVPVPRG HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV
     AATGGLHEFA DSQFGHCFSW GENREEAISN LVVALKELSI RGDFRTTVEY LVKLLETESF
     QANETDTSWL DHLIAEKVQA EKPDTILGVV CGALNVADAL FRTSMDDFLH SLERGQVLPA
     ASLLNIVDVE LIYEGMKYSL KVARQSLSTY VIIMNNTHIE IDVHRLNDGG LLLSYDGNSY
     TTYMKEETDR YRITIGNKTC DFEKENDPTL LRSPSAGKLL QYTVDDGGHV CVGHSYAEIE
     VMKMVVTLAV EESGLIHYVK RPGTLLETGC VVARLELDNP TKVHLAQLYT GGLHTQQPLP
     ILGEKLHQVF HNVLESLMNV MNGYCLPEPY FSTKLKEWVF KLMKTLRDPS LPLLELQEIM
     TSISGRIPPS VEKSIRKVMA QYASNITSVL CQFPSQQIAS ILDSHAATLQ RKADREVFFL
     NTQSIVQLVQ RYRSGIRGHM KSVVLDLLRC YLQVETQFQQ AHYDKCVIHL REQYMPDMTP
     VLECIFSHAQ VAKKNLLVTM LIDHLCGRDH TLTDELMAIL NELTQLSKTE HSKVALRARQ
     VLIASHLPSY ELRHNQVESI FLSAIDMYGH QFCPENLKKL ILSETTIFDV LPTFFYHSNQ
     VVRMAALEVY VRRAYIAYEL NSLQHRQLTD GTCVVEFQFM LPSSHPNRWA YISNPDLARH
     STELFMDSGF SPLCQRMGAM VAFDRFGDFT RSVKVMEFHF GVFRIGGLFS LKRRQGTKGM
     LLSVVLVSHF SSRRSPVLCS GGRGLLLVYD FCFPLQREFP KFFTFRARDK FAEDRIYRHL
     EPALAFQLEL NRMRNFDLTA VPCANHKMHL YLGAAKVEEG AEVTDYRFFV RAIVRHSDLI
     TKEASFEYLQ NEGERLLLEA MDELEVAFSN TSVRTDCNHI FLNFVPTVVM DPSKIEESVR
     SMVMRYGSRL WKLRVLQAEV KINIRLTPTA QAIPIRLFLT DESGYYLDIS LYKEVNDPST
     GNIMFHSYGD KQGPLHGMLI NTPYVTKDLL QSKRFQAQSL GTTYVYDFLE MFRQALFKLW
     GSTEADPADV LTYTELVLDS QGQLVQMNRL PGGNEIGMVA FKMKMKTPEY PRGRDIVVII
     NDITYKIGSF GPEEDLLFLR ASELARSEGI PRIYIAANSG ARIGFADEIK HKFQVGWVDP
     AEPYKGFKYL YLTPQEYTRI SSTNSVHCEH VEEAGESRYI ITDIIGKEEG FGVENLRASG
     TIAGESSLAY DEIVTISMVT CRAIGIGAYL VRLGQRVIQV ENSHIILTGA GALNKVLGRE
     VYTSNNQLGG VQIMHNNGVS HVTVPDDFEG VYTILQWLTF MPKDNRSPLP ITTTSDPIDR
     EIDFVPSKAP YDPRWMLAGR PHPTVKGSWQ SGFFDHGSFM EIMQPWAQTV VVGRARLGGI
     PVGVIAVETR TVELAVPADP ANPESEAKII QQAGQVWFPD SAFKTAQAIR DFDRERLPLL
     IFANWRGFSG GMKDMYDQVL KFGAYIVDSL RQFKQPALVY IPPHAELRGG SWVVIDPTIN
     PLHMELYADK ESRGGILEAE GTVEIKFRRK ELLKTMRRID ATYARIAEQL GSLRLSAEEH
     KELEKQLKAR EDYLLPIFHQ VAVQFADLHD TPGRMQEKGV VTVKPWGFFF SLPNSLFFQP
     LESDHPSCLR RCRNCFSFHS SWKNKGWNPC STNACCISFV LHLTLTSLTG LS
//

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