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Database: UniProt
Entry: Q6CC91_YARLI
LinkDB: Q6CC91_YARLI
Original site: Q6CC91_YARLI 
ID   Q6CC91_YARLI            Unreviewed;      2266 AA.
AC   Q6CC91;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 134.
DE   SubName: Full=YALI0C11407p {ECO:0000313|EMBL:CAG82031.1};
GN   ORFNames=YALI0_C11407g {ECO:0000313|EMBL:CAG82031.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG82031.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG82031.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382129; CAG82031.1; -; Genomic_DNA.
DR   RefSeq; XP_501721.1; XM_501721.1.
DR   SMR; Q6CC91; -.
DR   STRING; 284591.Q6CC91; -.
DR   EnsemblFungi; CAG82031; CAG82031; YALI0_C11407g.
DR   GeneID; 2909424; -.
DR   KEGG; yli:YALI0C11407g; -.
DR   VEuPathDB; FungiDB:YALI0_C11407g; -.
DR   HOGENOM; CLU_000395_5_1_1; -.
DR   InParanoid; Q6CC91; -.
DR   OMA; DFEDNTI; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000001300}.
FT   DOMAIN          66..575
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          224..416
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          702..776
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1523..1858
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1863..2175
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          441..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2266 AA;  251115 MW;  8B581AF5F9374E4A CRC64;
     MRLQLRTLTR RFFSMASGSS TPDVAPLVDP NIHKGLASHF FGLNSVHTAK PSKVKEFVAS
     HGGHTVINKV LIANNGIAAV KEIRSVRKWA YETFGDERAI SFTVMATPED LAANADYIRM
     ADQYVEVPGG TNNNNYANVE LIVDVAERFG VDAVWAGWGH ASENPLLPES LAASPRKIVF
     IGPPGAAMRS LGDKISSTIV AQHAKVPCIP WSGTGVDEVV VDKSTNLVSV SEEVYTKGCT
     TGPKQGLEKA KQIGFPVMIK ASEGGGGKGI RKVEREEDFE AAYHQVEGEI PGSPIFIMQL
     AGNARHLEVQ LLADQYGNNI SLFGRDCSVQ RRHQKIIEEA PVTVAGQQTF TAMEKAAVRL
     GKLVGYVSAG TVEYLYSHED DKFYFLELNP RLQVEHPTTE MVTGVNLPAA QLQIAMGIPL
     DRIKDIRLFY GVNPHTTTPI DFDFSGEDAD KTQRRPVPRG HTTACRITSE DPGEGFKPSG
     GTMHELNFRS SSNVWGYFSV GNQGGIHSFS DSQFGHIFAF GENRSASRKH MVVALKELSI
     RGDFRTTVEY LIKLLETPDF EDNTITTGWL DELISNKLTA ERPDSFLAVV CGAATKAHRA
     SEDSIATYMA SLEKGQVPAR DILKTLFPVD FIYEGQRYKF TATRSSEDSY TLFINGSRCD
     IGVRPLSDGG ILCLVGGRSH NVYWKEEVGA TRLSVDSKTC LLEVENDPTQ LRSPSPGKLV
     KFLVENGDHV RANQPYAEIE VMKMYMTLTA QEDGIVQLMK QPGSTIEAGD ILGILALDDP
     SKVKHAKPFE GQLPELGPPT LSGNKPHQRY EHCQNVLHNI LLGFDNQVVM KSTLQEMVGL
     LRNPELPYLQ WAHQVSSLHT RMSAKLDATL AGLIDKAKQR GGEFPAKQLL RALEKEASSG
     EVDALFQQTL APLFDLAREY QDGLAIHELQ VAAGLLQAYY DSEARFCGPN VRDEDVILKL
     REENRDSLRK VVMAQLSHSR VGAKNNLVLA LLDEYKVADQ AGTDSPASNV HVAKYLRPVL
     RKIVELESRA SAKVSLKARE ILIQCALPSL KERTDQLEHI LRSSVVESRY GEVGLEHRTP
     RADILKEVVD SKYIVFDVLA QFFAHDDPWI VLAALELYIR RACKAYSILD INYHQDSDLP
     PVISWRFRLP TMSSALYNSV VSSGSKTPTS PSVSRADSVS DFSYTVERDS APARTGAIVA
     VPHLDDLEDA LTRVLENLPK RGAGLAISVG ASNKSAAASA RDAAAAAASS VDTGLSNICN
     VMIGRVDESD DDDTLIARIS QVIEDFKEDF EACSLRRITF SFGNSRGTYP KYFTFRGPAY
     EEDPTIRHIE PALAFQLELA RLSNFDIKPV HTDNRNIHVY EATGKNAASD KRFFTRGIVR
     PGRLRENIPT SEYLISEADR LMSDILDALE VIGTTNSDLN HIFINFSAVF ALKPEEVEAA
     FGGFLERFGR RLWRLRVTGA EIRMMVSDPE TGSAFPLRAM INNVSGYVVQ SELYAEAKND
     KGQWIFKSLG KPGSMHMRSI NTPYPTKEWL QPKRYKAHLM GTTYCYDFPE LFRQSIESDW
     KKYDGKAPDD LMTCNELILD EDSGELQEVN REPGANNVGM VAWKFEAKTP EYPRGRSFIV
     VANDITFQIG SFGPAEDQFF FKVTELARKL GIPRIYLSAN SGARIGIADE LVGKYKVAWN
     DETDPSKGFK YLYFTPESLA TLKPDTVVTT EIEEEGPNGV EKRHVIDYIV GEKDGLGVEC
     LRGSGLIAGA TSRAYKDIFT LTLVTCRSVG IGAYLVRLGQ RAIQIEGQPI ILTGAPAINK
     LLGREVYSSN LQLGGTQIMY NNGVSHLTAR DDLNGVHKIM QWLSYIPASR GLPVPVLPHK
     TDVWDRDVTF QPVRGEQYDV RWLISGRTLE DGAFESGLFD KDSFQETLSG WAKGVVVGRA
     RLGGIPFGVI GVETATVDNT TPADPANPDS IEMSTSEAGQ VWYPNSAFKT SQAINDFNHG
     EALPLMILAN WRGFSGGQRD MYNEVLKYGS FIVDALVDYK QPIMVYIPPT GELRGGSWVV
     VDPTINSDMM EMYADVESRG GVLEPEGMVG IKYRRDKLLD TMARLDPEYS SLKKQLEESP
     DSEELKVKLS VREKSLMPIY QQISVQFADL HDRAGRMEAK GVIREALVWK DARRFFFWRI
     RRRLVEEYLI TKINSILPSC TRLECLARIK SWKPATLDQG SDRGVAEWFD ENSDAVSARL
     SELKKDASAQ SFASQLRKDR QGTLQGMKQA LASLSEAERA ELLKGL
//
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