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Database: UniProt
Entry: V5EU37_KALBG
LinkDB: V5EU37_KALBG
Original site: V5EU37_KALBG 
ID   V5EU37_KALBG            Unreviewed;      2182 AA.
AC   V5EU37;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Acetyl CoA carboxylase {ECO:0000313|EMBL:EST08865.1};
GN   ORFNames=PSEUBRA_SCAF14g01620 {ECO:0000313|EMBL:EST08865.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST08865.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
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; KI545856; EST08865.1; -; Genomic_DNA.
DR   RefSeq; XP_016293854.1; XM_016434806.1.
DR   STRING; 1365824.V5EU37; -.
DR   GeneID; 27417413; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_2_1; -.
DR   OMA; DFEDNTI; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000019377; 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: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:UP000019377}.
FT   DOMAIN          38..546
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          195..387
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          673..747
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1455..1791
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1795..2110
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2182 AA;  239580 MW;  93AB30DFA1BC8048 CRC64;
     MPPPDHKAVS HFIGGNPLET APAGAVTDFI RKQGGHSVIT KVLICNNGIA AVKEIRSIRK
     WAYETFGNER AIEFVVMATP EDLKVNADYI RMADQYVEVP GGSNNNNYAN VDLIVDVAER
     AGVHAVWAGW GHASENPRLP ESLAASKHKI IFIGPPGSAM RSLGDKISST IVAQHADVPC
     MPWSGTGIKE TIMSEQGFLT VSDDVYQKAC IHTAEEGLEK AEKIGYPVMI KASEGGGGKG
     IRKCTNGEDF KQLYNAVLGE VPGSPVFVMK LAGQARHLEV QLLADQYGNA ISIFGRDCSV
     QRRHQKIIEE APVTIAPEDA RESMEKAAVR LAKLVGYVSA GTVEWLYSPD SGEFAFLELN
     PRLQVEHPTT EMVSGVNIPA AQLQVAMGIP LYSIRDIRTL YGMDPRGNEV IDFDFASPES
     FKTQRKPQPQ GHVVACRITA ENPDTGFKPG MGALTELNFR SSTSTWGYFS VGTSGALHEY
     ADSQFGHIFA YGADRSEARK QMVISLKELS IRGDFRTTVE YLIKLLETDA FESNKITTGW
     LDGLIQDRLT AERPPADLAV ICGAAVKAHL LARECEDEYK RILNKGQVPP RDTIKTVFSI
     DFIYENVKYN FTATRSSVSG WVLYLNGGRT LVQLRPLTDG GLLIGLTGKS HPVYWREEVG
     MTRLMVDSKT CLIEQENDPT QIRSPSPGKL VRFLVESGDH VKAGQAIAEI EVMKMYLPLV
     AAEDGVVSFV KTAGVALSPG DIIGILSLDD PSRVQHAKPF AGQLPDFGLP IIIGSKPHQR
     YSYLVEVIND ILDGYDQSFR MQAVIKELME TLRNPELPYG QASQILSSLG GRIPARLEDV
     VRNTIEMGHS KNVEFPAARL RKLTENFLRD SVDPAIRGQV QITIAPLYQL FEAYAGGLKA
     HEGNVLASFL QKYYDIESKF TGEADVVLEL RLQADGDLDK VVALQTSRNG LNRKNALLLT
     LLDKHIKGTS LVSRTSGAQM IEALRKLASL QGKSTAPVAL KAREVSLDAD MPSLADRSAQ
     MQAILRGSVT SSKYGGDDEY HAPSLEVLRE LSDSQYSVYD VLHSFFGHRE HHVAFAALCT
     YVVRAYRAYE IVNFDYAIED FDVEERAVLT WQFQLPRSAS SLKERERQVS ISDLSMMNST
     RKTVAPAELR TGAMTSCVDV SDIPDLLPKV LKFFKSSGGS PINVLNVAVV DQADFVDAEV
     RSKLAQYTNA CSKQFAAARI RRVTYLLCQP GMYPFFATFR PSEHGIWTEE KAIRNIEPAL
     AYQLELDRVS KNFELTPVPV SSSTIHLYFA RGIQNSADTR FFVRSLVRPG RVQGDMAAYL
     VSESDRIVND ILNVIEVALG QPEYRTADAS HIFMSFIYQL DVSLEDVQKA IAGFLERHGT
     RFFRLRITGA EIRMILSGPN GEARPIRAFV HNETGLVVRY ETYEENAADD GSVVLRAIEP
     QGKEASLNGQ SAHFPYTTKV ALQSRRSRAH ALQTTFVYDF IDVLGQAVRA SWRKVAASKT
     PSEVIKSAVE LVFDEQENLR ELKRAPGMNN IGMVAWLVEV ATPEFPAGRK LVVVGNDVTI
     QAGSFGPVED RFFAAASKLA RELGVPRLYI SANSGARIGL ATEALDLFKV KFVGDDPAKG
     FEYLYLDDDS LHVLQTKAPN SVMTKPLKAA DGSNHNVITD VIGKPQEGLG VECLSGSGLI
     AGETSRAKDQ IFTATIVTGR SVGIGAYLAR LGERVIQVEG SPLILTGYQA LNKLLGREVY
     TSNLQLGGPQ IMYKNGVSHL TAQDDLDAVK AFVNWMSYVP AQRGGPLPIM PTTDTWDRAV
     TYQPPRGPYD PRWLINGTRD ESGAKLTGLF DDGSFVETLG GWATSVVTGR ARLGGIPVGV
     IAVETRTLER VVPADPANPS STEQRIMEAG QVWYPNSAYK TAQAIWDFDK EGLPLVILAN
     WRGFSGGQQD MYDEILKQGS KIVDGLSAYK QPVFVHIPPM GELRGGSWVV VDSAINDNGM
     IEMSADVNSA RGGVLEASGL VEIKYRADKQ RATMQRLDSV YAKLSKEAAE ATDFTAQTAA
     RKALAEREKQ LSPIFTAIAT EYADAHDRAG RMLATGVLRS ALPWENARRY FYWRLRRRLT
     EVAAERTISE ANPLLKHVER VAALRQFTGA AASDDDKAVA EHMEASAAQL LAATKQLKAQ
     YILAQISTLD PELRAQLAAS LK
//
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