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Database: UniProt
Entry: F6URY7_XENTR
LinkDB: F6URY7_XENTR
Original site: F6URY7_XENTR 
ID   F6URY7_XENTR            Unreviewed;      2329 AA.
AC   F6URY7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 3.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN   Name=acaca {ECO:0000313|Ensembl:ENSXETP00000019619};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000019619};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000019619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000019619};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000019619}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) 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; ENSXETT00000019619; ENSXETP00000019619; ENSXETG00000008955.
DR   Xenbase; XB-GENE-1013637; acaca.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_0_1; -.
DR   TreeFam; TF300061; -.
DR   UniPathway; UPA00655; UER00711.
DR   Bgee; ENSXETG00000008955; Expressed in brain and 12 other cell types or tissues.
DR   ExpressionAtlas; F6URY7; baseline.
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   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
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   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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          121..622
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          275..470
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          749..823
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1558..1896
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1900..2216
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2329 AA;  263211 MW;  28E819618AC4F8BE CRC64;
     MGHFFPPDPP LSKLLDQHSR FIIGSVSEDN SEDEFSSMVR VDLEDKERSS SPASIASTAS
     DTLSDMGLSN YQDNLALQMR PSMSGLHLVK QGRDRKKIDL QRDFTVASPA EFVTRFGGNK
     VIEKVLIANN GIAAVKCMRS IRRWSYEMFR NERAIRFVVM VTPEDLKANA EYIKMADHYV
     PVPGGPNNNN YANVELILDI AKRIPVQAVW AGWGHASENP KLPELLLKNG IAFMGPPSQA
     MWALGDKIAS SIVAQTAGIP TLPWSGSGLK VDWQESDLKK STLIVPPEVY GKGYVKDVDD
     GLKAAEVVGY PVMIKASEGG GGKGIRKVNN AEDFPNLFRQ VQAEVPGSPI FVMRLAKQSR
     HLEVQILSDQ YGNAISLFGR DCSVQRRHQK IIEEAPASIA TATIFEQMEQ CAVKLAKMVG
     YVSAGTVEYL YSQDGSFYFL ELNPRLQVEH PCTEMVADVN LPAAQLQIAM GVPLHRIKDI
     RMLYGLPAWG DSPIDFDNSL NAPCPRGHVI AARITSENPD EGFKPSSGTV QELNFRSNKN
     VWGYFSVAAA GGLHEFADSQ FGHCFSWGEN REEAISNMVV ALKELSIRGD FRTTVEYLIK
     LLETESFQNN RIDTGWLDRL ISEKVQAERP DAMLGVVCGA LHVADVTFRN SVSNFLHSLE
     RGQVLPAHTL LNTVDVELIY EGEKYVLKVT RQSPNSYVVI MNNSCVEVDV HRLSDGGLLL
     SYDGSSYTTY MKEEVDRYRI TIGNKTCVFE KENDPSILRS PSAGKLIQYV VEDGGHVFAG
     QCYAEIEVMK MVMTLTAVES GCIHYVKRPG AALEPGCVIA KLQLDDPSRV QQAELHRGPL
     PLIHSTALRG EKLHRVFHCV LDNLVNVMNG YCLPEPYFSS KLKDWVERLM KTLRDPSLPL
     LELQDIMTSV SGRIPPNVEK SIKKEMAQYA SNITSVLCQF PSQQIANILD SHAATLNRKS
     DREVFFMNTQ SIVQLVQRYR SGIRGHMKAV VMDLLRQYLK VETQFQHGHY DKCVFALREE
     NKSDLTMVLN SIFSHAQVTK KNLLITMLID QLCGRDPTLT DELLNILMEL TQLSKTTNAK
     VALRARQVLI ASHLPSYELR HNQVESIFLS AIDMYGHQFC IENLQKLILS ETSIFDVLPN
     FFYHSNQVVR MAALEVYVRR AYIAYELNSV QHRQLKDNTC VVEFQFMLPT SHPNRMSFSS
     NLNHYGMVHV VSDVLLDTSF TPPCQRMGGM VAFRTFEDFV RLFDDVMSCF SDSPPQSPVF
     PEAGHPSLYD EDDNKVPINE PIHILNVAIK TDCDIDDDGL AAMFREFTQS KVTFFPCCLF
     LCLAFLFLHK DFRKQVNCEV DQRFQFEEDR IYRHLEPALA FQLELNRMRN FDLTAIPCAN
     HKMHLYLGAA KVEVGTEVTD YRFFVRAIIR HSDLVTKEAS FEYLQNEGER LLLEAMDELE
     VAFNNTNVRT DCNHIFLNFV PTVIMDPSKI EESVRSMVMR YGSRLWKLRV LQAELKINIR
     LTPTGKQIPI RLFLTNESGY YLDISLYKEV TDSRTAQIMF QAYGDKQGPL HGMLINTPYV
     TKDLLQSKRF QAQSLGTTYV YDIPEMFRQA LIKLWESMEA HAFLPKSPLP SDVLTYTELV
     LDDQGQLVHM NRLPGGNEIG MVAWKMTLKS PEYPDGRDII VIGNDITYKI GSFGPQEDLL
     YLRASELSRS EGIPRIYVAA NSGARIGLAE EIRHMFHVAW EDPADPYKGF KYLYLTPQDY
     KKVSALNSVH CEHVEDEGES RYKITDIIGK EEGLGVENLR GSGMIAGESS LAYEEIITIN
     LVTCRAIGIG AYLVRLGQRT IQVENSHIIL TGAGALNKVL GREVYTSNNQ LGGIQIMHNN
     GVTHSTVYDD FEGVYTILQW LSYMPKCVAS PVPILTPKDS IERLIEFTHT KAPYDPRWML
     AGRPHPTQKG QWLSGFFDYG SFMEIMQPWA QTVVVGRARL GGIPVGVVAV ETRTVELSVP
     ADPANLDSEA KIIQQAGQVW FPDSAFKTAQ AIKDFNREGL PLMVFANWRG FSGGMKDMYD
     QVLKFGAYIV DGLREYRQPV LVYIPPQAEL RGGSWVVIDP TINPRHMEMY ADKESRGGVL
     EPEGTVEIKF RRKDLIKTMR RVDPVYIHLA EKLGTPELGA ADCKELETKL KEREEFLLPI
     YHQVAVQFAD LHDTPGRMQE KGVITDVIEW KTSRTFFYWR LRRLLLENVA KKKIHSANPE
     LTDGQIQAML RRWFVEVEGT VKAYLWDNNK DVVEWLEKQM AEEEGTRSVV DENIKYISRD
     YILKQIRSLV QENPEVAMDS IVHMTQHISP TQRAEIVRIL STMDSPTSS
//
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