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
//