UniProt: A0A3L8SC52

Database: UniProt
Entry: A0A3L8SC52_CHLGU

LinkDB:  A0A3L8SC52_CHLGU 
Original site:  A0A3L8SC52_CHLGU

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (32)   
   InterPro (17)   
   Pfam (7)   
   PROSITE (7)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (41)   

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ID   A0A3L8SC52_CHLGU        Unreviewed;      2289 AA.
AC   A0A3L8SC52;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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   ORFNames=DV515_00009379 {ECO:0000313|EMBL:RLV99801.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Passeroidea; Passeridae; Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV99801.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV99801.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV99801.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV99801.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
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   -!- 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:RLV99801.1}.
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DR   EMBL; QUSF01000030; RLV99801.1; -; Genomic_DNA.
DR   STRING; 44316.ENSEGOP00005016364; -.
DR   OrthoDB; 14612at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
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; 2.40.50.100: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; 4.
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; 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; 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; 2.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 3.
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:UP000276834}.
FT   DOMAIN          77..579
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          236..427
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          695..769
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1545..1801
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1805..2176
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2289 AA;  257544 MW;  EC6E08FDDA775316 CRC64;
     MATAFRVGRR RSSLAGVGGT VPEPLSVSAL LEPSAGIRPS MSGLNLAKKS HRKMDLQRDF
     SVASPAEFVT RFGGNRVIEK VLIANNGIAA VKCMRSIRRW AYEMFRNERA IRFVVMVTPE
     DLKANAEYIK MADHYVPVPG GTNNNNYANV ELIVDISKRI PVQAVWAGWG HASENHKLPE
     LLQKNGIAFL GPPSDAMWAL GDKVASTIVA QTLEIPTLPW SGSGLVAQWS EEDQDHQQAI
     SIPLETYAQG CVKDVEEGLE VAMRIGYPLM IKAAEGGGGK GIRKVEAAEE FSACFRQVQA
     EAPGSPIFLM QLAQHARHLE VQVLADEYGN AISLFSRDCS IQRRHQKIIE EAPATIAAPA
     VTEMMEKCAV RLAQMAGYVS AGTVEYLYGE DGSFHFLELN PRLQVEHPCT EMVADVNLPA
     AQLQIAMGIP LHRIKDIRVL YGESPWGDTP ICFHSPSSTP VPRGHVIAAR ITSENPEEGF
     KPSSGTVQEL NFRSSKNVWG YFSVAAAGGL HEFADSQFGH CFSWGENREE ATSNMVVALK
     ELSIRGDFRT TVEYLIKLLE TESFQNNEIH TGWLDHLIAE KVQAEKPDTM LGVVCGALNV
     ADAAFRTGQV LPAASLLNIV DVELLYEGVK YILQVARQSL TTYVVIMNRT HIEIDVHRLN
     DGGLLLSYDG CSYTTYMKEE IDRYRITIGN KTCTFEKEKD PTVLRSPSAG KLLQYTVEDG
     GHVDEGKVYA EIEVMKIIMT LAVEEAGQLH YVKRPGALLE AGCIIARLQL DDPSKVKPAQ
     PFTGGLPVQQ TLPITGEKQH QVLRNVLDNL TNIMNGYCLP EPYFKTKVKE WVAQLMKTLR
     DPALPLLELQ EIMTSISGRI PLAVEKSIRK VMAQYASNIT SVLCCFPSQQ IANVLDTHAA
     TLQRKAEREV FFMNTQSLVQ LVQRYRSGIR GYMKAVVLDL LRRYLQVETQ FQHAHYDKCV
     ISLREQCKPN MNPVLESIFS HAQVAKKNQL VIMLIDQLCG RDPTLTDELT TILHELTQLS
     KTEHSKVALR ARQVLIASHM PSYELRHNQV ESIFISAIDM YGHEYCPENL KKLILSETSI
     FDVLPVFFYH TNKVVRMAAL EVYVRRGYIA YELHSLQHQQ LSDGTCLVEF KFMLPSSHPN
     RMSAPISISN PDLARHSTEL FMDSGFSPTS QRMGVMVAFR RFEDFTRNFD EVISCFANSP
     SDSGLLSDAQ ATTYDEEDTK NIREEPIHIL NIALCSADHM EDEKLVPIFR AFAQSKKNIL
     VDRGLRRITF LIAQQREFPK FFTFRARDEF AEDRIYRHLE PALAFQLELS RMRNFDLTAI
     PCANHKMHLY LGAARVQAGT EATDYRFFIR AIVRHSDLIT KAGWRRGASG HEASFEYLQN
     EGERLLLEAM DELEVAFNNT IVRTDCNHIF LNFVPTVIMD PSKIEESVRS MVMRYGSRLW
     KLRVLQAEVK INIRLTPTAT AIPIRLFLTN ESGYYLDISL YKEVRDLSTG SIMFQSYGDK
     QGPQHGMLIN TPYVTKDLLQ AKRFQAQSLG TTYVYDFPEM IRQVGMVAFK MKLKTPEYPK
     GRDIVLICND ITHKIGSFGP EEDLVFLRAS ELARAEGIPR IYIAANSGAR IGFADEIKHM
     FQVAWVDPAE PYKGFRYLYL TPQDYTRIST MNSVRCEHVE EGGESRYVLL DIIGKDNGFG
     VENLRAAGTI AGESSRAYDE IVTISMVTCR AIGIGAYLVR LGQRVIQVEN SHIILTGVTA
     LNKVLGREVY TSNNQLGGVQ IMHNNGVSHV TVPDDFEGVY TILQWLSYIP KDNQSPVPVT
     AISDPVEREI DFVPSKVPYD PRWMLAGRPH PTLKGTWQSG FFDQGSFMEI MKPWAQTVVV
     GRARYCREQG VELGSCLCGP SPSSPGCGTA FGMVEREQLS VGLGGRKTGL AEPSLPCHRL
     GGLPVGVIAV ETRTVEVTIP ADPANLDSEA KIIQQAGQVW FPDSAFKTAQ AIRDFNREHL
     PLMIFANWRG FSSGMKDMYD QMLKFGAFIV DSLRDFKQPV LVYIPPHAEL RGGSWVVIDA
     TINPLHVELY ADKESRGGIL EPGGTVEIKF RKKDLVKTMR RIDTVYAKLV EQLGTPELSE
     AQRKQLEKQL KAREELLLPV YHQVAVRFAD LHDTPGRMQE KGVITDILEW KSSRSFLYWR
     LRRLLLEEMV KGEVLKANSE LSHIHIQSML RRWFMETEGA EKGYLWDNNQ VVVEWLEKHM
     QEEDSTQSAI RENIKYLKRD YILKHIRSLL QANPELTMDC MVQMAQHITR PQKAQVAHLL
     SRVDTDDPS
//

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