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Database: UniProt
Entry: A0A0L0DL93_THETB
LinkDB: A0A0L0DL93_THETB
Original site: A0A0L0DL93_THETB 
ID   A0A0L0DL93_THETB        Unreviewed;      2241 AA.
AC   A0A0L0DL93;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:KNC52811.1};
GN   ORFNames=AMSG_08705 {ECO:0000313|EMBL:KNC52811.1};
OS   Thecamonas trahens ATCC 50062.
OC   Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX   NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC52811.1, ECO:0000313|Proteomes:UP000054408};
RN   [1] {ECO:0000313|EMBL:KNC52811.1, ECO:0000313|Proteomes:UP000054408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC52811.1,
RC   ECO:0000313|Proteomes:UP000054408};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA   Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000861};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC         CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001455};
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   EMBL; GL349475; KNC52811.1; -; Genomic_DNA.
DR   RefSeq; XP_013755120.1; XM_013899666.1.
DR   STRING; 461836.A0A0L0DL93; -.
DR   EnsemblProtists; KNC52811; KNC52811; AMSG_08705.
DR   GeneID; 25567336; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000054408; Unassembled WGS sequence.
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:SF3; ACETYL-COA CARBOXYLASE; 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   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:UP000054408}.
FT   DOMAIN          27..511
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          181..371
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          637..711
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1495..1840
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1845..2160
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2241 AA;  239265 MW;  F18543655D17D386 CRC64;
     MASVRGPALG TYPDVESYVK AKGGSRVIRK CLVANNGIAA VKTIRSVRDW AYTTFGSESA
     IQFVVMVTPE DLAANAAYIR MAEEAIEVPG GTNNNNYANV DQIVDVAIKA GVDAVFAGWG
     HASENPKLPD ALDAAGIVFI GPSGDAMRAL GDKIASTIVA QSVDVPCLPW SGDSLQLPED
     SAGATTVPAD LLAKACVTSA ADASDAAERI GYPVMIKASE GGGGKGIRMV QSADTVVDAF
     RQVAAEVPGS PIFIMKLAPS ARHLEVQLLC DMHGNAMSLF GRDCSMQRRH QKVLEEGPVT
     VATVDQQIAM EAAAVRLAKQ VNYVSAGTVE YLYFDDAHFF LELNPRLQVE HPVTEMITGV
     SIPASQLQVA MGIPLFAIPE IRVFYGLDPN ETAPFDLSAR PEPSCAVIAA RITAENAEEG
     FKPTSGLITD LSFASTTNVW GYFSVSAGSS LHEYSDSQFG HLFASGPPAR TPNVVIRGEI
     RTPVEYLANV LETPEFVDNT FSTAWLDARI RSGLLHRTVN LDEVFCGALA RVHAAATKRA
     NEFEAALARG QIPPLSLLDN NYAVTLIFNS VKYELSAVHT AKSSYALTLN GATASAELVE
     LVDGTFLVHM DGKTHTLYAR EEASGLRIVV NGRTCVFSDE FDPSLIRSLT PGKIVKFLVD
     DNSHVAVGEP IAHVEVMKMI MPMAAPAAGV ISFSKSEGSI LAPGMVIATL DLDDVSAVER
     ASPYDGAPPA FGPPRPLPTK PHKELELAAE VIAAAFDGYS PSNLSDAVAL FVKALGDPKL
     ALCQVSELLA SIESRLPDTL FASLTALLDS FEAAADAADA AGNPAPAFPA NELLAAIDAT
     EAGLAPKRSR ALPHASGASA YAVSRVKALM DQYISVETQY GQSNTRREEV LWDLRDENKD
     DVDRVVGLAR SHSGLENKNA VLGALLACVA ELRDCDLPVK PRAYVSIRGA TSPSARAQIG
     CVEDYQSQLE ALASFTGKGH ARLALASRVL LIHANLPSFA ERKAAMGELL ASVAGASPDE
     HHGLLTRLVD RPSSLSDVLV PFFTDPATAF ADLALKAYII RTYRAYDVLE FVPVVPEGVE
     SLVAAVAFHF NLPVRKSRPM TPSSRNSSAS SMDAASVSAT SSSGHLATRT SVAGFHSSPS
     MTAISEMASL PLPSPSGNSG EHRYGVMYAV NGGMDALYAS ADALLAAYTP PAHTLGFPAS
     SPLSFVNIIN FIVAVEGPLA PGQAEAAAAA FGTFLQDAAR SATLRELCVR RITLGLVVEG
     SYPVFFTYRG HLEYAEDGIH RYIEPPLAFQ LDIGRLSNYN IRAVPTGHSH LHVYAAHAKG
     APAGTAERIF VRSIVRDPES FTAAATVDLL ATEGERILVD ALDAIQMINV THPNLASADS
     NHIFINLLPN MVISLDEVRA IGARFVQAHG RRMFQLRVME TELKLNLQFA GSPDPDAFVP
     VRIQIKSRSG FVVRYHVYVE TLGDAPNGTP IFTAISQPGA LAEPAPWNGL PISTPYALPN
     PEQAARRRAQ NLDTVYIYDF PEVMDQAVRQ VWGRHVTAVV EAGEAPPTIP AVCCEATEYR
     LGADGKLAAW PNAFDASAPP PRIGMVAWKC VWYTPECPAG RVVVVVGNDI TCLQGSFGPA
     EDELFFQASA MARSLGVPRV YLSANSGARI GMAEELRAKF KVAWLDSTAP ERGAEYLYLE
     LDDAAELGND VVHWEEVDGP DGTRVARIVD IIGTADGIGV ENLRASGMIA GETSLAYEDV
     FTISLVSGRS VGIGAYLVRL GQRIVQHKSP PILLTGAGAL NKLLGSQVYT SNNQLGGIKI
     MHANGVSHLV CENNLDGVRD IVKWISYVPA VRDGPLPCLP SPVDGWDRDI AYTLPPSGAA
     DPRAMLAGAS AADGWVSGFF DRDSFVETLA GWARTVVTGR ARLGGMPVGV IAVETRSVTT
     VAPADPGDKT SQEMVYPEAG QVWYPNSASK TAQAINDFNF GEQLPLFIFA NWRGFSGGMR
     DMFNEVLKFG SHIVDALRKY KQPISIYIPP NGELRGGAWV VLDTTINADM IEMYASESAR
     GGILEPAGAV EIKYKERHLR ATMLRLDDEC KRLAEELAAA DAGSDAATAA AAALTARQDD
     LMPYYRQVAV QFADLHDTPG RMLAKGVVKS VVPWRNARRF FYWRMSRRVG LHGLARKLVA
     GNAATSYAAA VDMLHAWIAA AGVDLDNDRA VAEYVAIHRA DLDARVSTAD LAVARGLAGK
     LRTLLAGLSD DERAAVMAEL N
//
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