ID C5DBX3_LACTC Unreviewed; 2230 AA.
AC C5DBX3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=KLTH0A06050p {ECO:0000313|EMBL:CAR21280.1};
GN OrderedLocusNames=KLTH0A06050g {ECO:0000313|EMBL:CAR21280.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21280.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR21280.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928165; CAR21280.1; -; Genomic_DNA.
DR RefSeq; XP_002551722.1; XM_002551676.1.
DR STRING; 559295.C5DBX3; -.
DR GeneID; 8290526; -.
DR KEGG; lth:KLTH0A06050g; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; C5DBX3; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000002036; Chromosome A.
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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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:UP000002036}.
FT DOMAIN 59..568
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 217..409
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 1483..1819
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1823..2138
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1195..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2230 AA; 248754 MW; B172C996F7AD1F57 CRC64;
MSEESLSEVG VSQKDQYEVT DYTSKHASLA PHFLGLNTVE KAEDSPLKEF VKCHGGHTVI
SKVLIANNGI AAVKEIRSVR KWAYETFGNE RAVQFVAMAT PEDLEANAEY LRMADQYVEV
PGGTNNNNYA NVDLIVEIAE RADVDAVWAG WGHASENPLL PERLAKSPRK VIFIGPPGNA
MRSLGDKISS TIVAQHASVP CIPWSGTGVD QVHLDKENGL VSVTDDVYQK GCCDSPEDGL
AKAKQIGFPV MVKASEGGGG KGIRKVEREE DFIPLYKQAA NEIPGSPIFI MKLAGKARHL
EVQLLADQYG TNISLFGRDC SVQRRHQKII EEAPVTIAKP DTFSEMERSA VRLGKLVGYV
SAGTVEYLYS HDDDKFYFLE LNPRLQVEHP TTEMVTGVNL PAAQLQIAMG IPMHRVKDIR
LLYGVDPHTA TEIDFDFSSK DSKQIQRKPT PKGHCTACRI TSEDPNEGFK PSGGSLHELN
FRSSSNVWGY FSVSSSGGIH SFSDSQFGHI FAFGENRQAS RKHMVVALKE LSIRGDFRTT
VEYLIKLLET EDFEGNSITT GWLDDLISQK MTAEKPDPTL AVICGAATKV FIASENGRKE
FITSLQKGQV PNKSLLQTMY PVEFIHDGKR YKFTVAKSAD DRYTLFINGS KCEVGVRKLS
DGGLLIAVGG RSHTIYWKEE VSATRLSVDS MTTLLEVEND PTQLRTPSPG KLVKFLVENG
DHVNAGQPYA EVEVMKMQMP LVSQESGIVQ LLKQPGSTVS AGDILAILAL DDPTKVKHAM
PFEGMLPDMG APIVEGTKPA YKFRSLVSTL ENILNGYDNQ VIMNASLQQL IEVLRNPQLP
YSEWKMQSSA LHSRLPIKLD EQLEQLVNRS LSRNAHFPAR QLGKMLEAAQ KESDDPLFGT
VIEPLLDIST RYADGLEAHE HSVFAKFLQN YYQVEKLFSG TNVREEDVIL KLRDENAENL
DRVALTVLSH SRVSAKNNLI LAILKHYQPL CKMSSEVSSR ISEPLKQIVE LESKATAKVA
LQAREILIQA ALPSVRERTD QIEHILRSSV VQTAYGAFDN KRTDPDLEIL KDLIDSNYVV
FDVLTQFLTH RDPSVAAAAA EVYIRRAYRA YTIGDLKHYN HANNAVVEWK FQLPSAAFAS
VPQMKSKLGM HRAISVSDLT YVSEGDNQPL RTGILIASTH LDDVDEGLSK GLQLVPHHTS
SSGPVPDRSG SNATLSNVAN VSVSSTDGFE SEEEVLRRLR EILDMNKQQL VEASIRRITF
IFGYEDGTYP KYFTFRGPSY AEDETIRHIE PALAFQLELG RMSNFNIKQL FTENRNIHVY
EATGKNSAVD KRFFTRGIIR TGRISDDITI QEYLTSEANR LMSNILDNLE VIDTSNSDLN
HIFIHFSAVF DVSPEDVEAA FGGFLERFGK RLLRLRVAAA EIRIIIKDPQ TGAPVPLRAL
INNVSGYVVK TELYTEVKNA QGEWVFKSLD KPGSMHLRPI ATPYPAKESL QPKRYKAHLM
GTTYVYDFPE LFRQATVSQW KKISPKTKLS DEFFIANELI EEEDGELTEI DREAGANTIG
MVAFKVTVKT PEYPRGRQFV IVANDITFKI GSFGPQEDAF FNKVTEYARK RGIPRIYLSA
NSGARIGVAE ELIPLFNVSW NDPENPAKGF QYLYLSSEGM AELKKQAKDA SVVTERVVED
GEERFVIKSI IGADDGLGVE CLKGSGLIAG ATSRAYKDIF TITLVTCRSV GIGAYLVRLG
QRAIQIEGQP IILTGAPAIN KLLGREVYSS NLQLGGTQIM YNNGVSHLTA EDDLAGVQKI
MEWLSYVPAR RDLPVPILET EDKWDREVDF TPSTSEPYDV RWMIEGRNTP EGFEYGLFDK
GSFQETLSGW AKGVVVGRAR LGGIPLGVIG VETRMVENMI PADPANPVST ESLIQEAGQV
WYPNSAFKTA QAINDFNYGE QLPLMIMANW RGFSGGQRDM YNEVLKYGSF IVDALVGYKQ
PIFTYIPPTG ELRGGSWVVV DPTINAEQME MYADVNSRAG VLEPEGMVGI KYRREKLLAT
MARLDETYKN LKTQMSDPGL SVEKHQEIAT KLAAREKMLM PIYHQITVQF ADLHDRSGRM
VAKGVISKEL DWPEARRFFF WRLRRRLNEE YLMKRLNTEL PNAPRLEKIA RLSSWYPASV
DREDDRIVAN WIEENYSVLE EHLKALKVES FAQNLAKSIR SDHENAISGL SEVLKLLSAE
DKAKILNSLK
//
