ID A0A1Q3DXL8_LENED Unreviewed; 2227 AA.
AC A0A1Q3DXL8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetyl-carboxylase {ECO:0000313|EMBL:GAV99741.1};
GN ORFNames=LENED_001220 {ECO:0000313|EMBL:GAV99741.1};
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353 {ECO:0000313|EMBL:GAV99741.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAV99741.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAV99741.1,
RC ECO:0000313|Proteomes:UP000188533};
RG Lentinula edodes genome sequencing consortium;
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAV99741.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAV99741.1,
RC ECO:0000313|Proteomes:UP000188533};
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RT "A genome survey and senescence transcriptome analysis in Lentinula
RT edodes.";
RL Submitted (FEB-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAV99741.1}.
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DR EMBL; BDGU01000018; GAV99741.1; -; Genomic_DNA.
DR STRING; 5353.A0A1Q3DXL8; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000188533; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 38..546
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 190..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 1467..1805
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1809..2123
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT COILED 2020..2047
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2227 AA; 246908 MW; C96A2F130E8B5D79 CRC64;
MSAYDHSRVQ YFIGGNSLDK ASPSSVYDFV KANGGHTIIT KVLIANNGIA AVKEIRSIRQ
WSYETFGSER QVEFTVMATP EDLKVNAEYI RMADRYIEVP GGSNNNNYAN VDLIVDVAER
AGVHAVWAGW GHASENPRLP ESLAASKNKI VFIGPPGSAM RSLGDKISST IVAQSADVPT
MPWSGTGITD TALSEAGYVI VPDKAYQDAC VTSVEEGLVK AEEIGWPVMI KASEGGGGKG
IRKVEQPEAF KNAYHAVAGE IPGSPIFIMK LAGAARHLEV QLLADQYGNA ISLFGRDCSV
QRRHQKIIEE APVTIAKQDT FEKMERAAVR LAKLVGYVSA GTVEYLYSHA DDSFHFLELN
PRLQVEHPTT EMVSGVNLPA AQLQVAMGIP LHRIRHIRQL YGVAPNAASE IDFEMIKPDA
NQLQRKPRPK GHVVAVRITA ENPDAGFKPS SGSLQELNFR SSTNVWGYFS VSSAGGLHEF
ADSQFGHIFA YGEDRGESRK NMIIALKELS IRGDFRTTVE YLIKLLELDD FKDNTITTGW
LDSLISDKLT AERPDATLAV ICGAVTKAYL ASEACWTEYK RILDKGQVPA RDVLKTVFVI
DFIYENVRYS FTAARSSSTA WTLYLNGGST MVGARPLADG GLLVLLDGRS HSIYWREEVG
ALRLMVDAKT CLIEQENDPT QLRSPSPGKL IRFFVDSGEH INAGEQYAEI EVMKMYMPLV
ASEDGIVQLI KQPGVSLEPG DILGILTLDD PGRVKHAKPF EGLLPTMGTP AVTGSKPHQR
FIRCLGVLND ILDGFDNQAI MASTVKDLID ILHDPELPYS ELTAILSSLS GRIPAKLDDS
IHAALETAKA KGEFPAARIK KVLENFVESS VLPQDRPMFR TQLGAIYDVL DRFTGGLKGH
EIKVWSNLLE KYEATERMFG GSIEARILTL REQNKDDLDK VISLVLSHIK VSSKAKLVLT
ILNHIKTKGI SVSNAESPLY KVLQDLASLE AKSSTSVSLK AREVLIMGQM PSYEERLGQM
ETVLKSSVTS QYYGEQVNTV HTPSAEVLRE LSDSRYTVFD VLSAFFEHED HMVPLAAFEV
YIRRAYKAYT LLSIDYEEGD ELDDGDSPSI VTWRFNLGQS HSPPSTPRIS LSGSASVSDL
TYLISRHQSQ PIRVGAISSF PNFLALAKGF SKVASALPLF DAIEYNSRYG NPQSPPNVLN
VALRLFREED DMPEDAWFEK LTAFVNEQSS TLRERGVGRV SIMLCRPSQY PVYLTLREVD
RVWTEEQSIR NIEPALAFQL ELSRLSNYKL KPVFVESKQI HIYHAVAREN QLDNRFFVRA
LVRPGRLRGS MSTAEYLISE TDRLVTTVLD ALELVTAEQR NTDCNHIFLN FIYNLAVTYE
DVLAAISGFI ERHGKRLWRL HVTGSEIRIA LEDDEGNVTP IRCVIENVSG FIVNYHGYQE
ITTDKGTTIL KSIGEKGPLH LQPVHQAYST KESLQPKRYQ AHLIGTTYVY DFPDLFSKAL
QNLWDSARAT SPTLVKPRVL LESKELVLDE HDQLAEVDRA PGNNTFGMIG WVFTMRTPEF
PQGRRVVVVA NDITYKIGSF GPIEDQFFYL VTQYARELGL PRIYLSANSG ARIGLAEELI
PLFSAAWNEE GHPEKGVHYL YLTHENYLKL EEQGHDSIKT VDVEVAGELR HKITDIIGLQ
DGLGVESLKG SGLIAGETSR AYDDIFTITL VTARSVGIGA YLVRLGERAV QVEGQPIILT
GAGALNKVLG REVYTSNLQL GGTQIMFKNG VSHLTASSDL EGATHILKWL SYVPEVKDGA
LPVLESSDSW DRDIGYTPPK GAYDPRWFIE GKTDEATSEW MSGFFDKGSF QETLSGWAQT
VVVGRARLGG IPMGVIAVET RTIERIVPAD PANPASFEQR IMEAGQVWYP NSAYKTAQAI
FDFNREGLPL IIFANWRGFS GGQQDMYDEV LKQGSKIVDG LSSYKQPIFV YIVPNGELRG
GAWVVLDPSI NSEQMEMYAD VDARAGVLEP EGIVEIKFRQ NKITALMERL DTEYASLKRE
SKDATKTAES RSAATAALER REAILQPTYK QIALLYADLH DRTGRMEAKG CAKPAIWKDA
RRKFYWAVRA RVARSAALAE LTEASPGSTT EYRSHLLDSL ASIDAAMNDR EMSETLEKLD
LSQTVSQLKA DYLMRRMVEL TKEDRKAAMN GFARLADNLS DEERNSLISV LQNATRSPAP
PSYATSS
//
