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
//