ID A0A165EPE4_9APHY Unreviewed; 2233 AA.
AC A0A165EPE4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acetyl CoA carboxylase {ECO:0000313|EMBL:KZT07489.1};
GN ORFNames=LAESUDRAFT_724944 {ECO:0000313|EMBL:KZT07489.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07489.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07489.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07489.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427619; KZT07489.1; -; Genomic_DNA.
DR SMR; A0A165EPE4; -.
DR STRING; 1314785.A0A165EPE4; -.
DR InParanoid; A0A165EPE4; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000076871; 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:UP000076871}.
FT DOMAIN 38..544
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 193..385
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 671..745
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1470..1808
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1812..2126
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 2211..2233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2233 AA; 247999 MW; 7E1691706FAD37DA CRC64;
MEKYDHSRAA QFIGGNTLDK APSGPVADFV KSHGGHTVIT KVLIANNGIA AVKEIRSIRQ
WSYETFGTER AVEFTVMATP EDLKVNAEYI RMADRYVEVP GGSNNNNYAN VDLIVDVAER
AGVHAVWAGW GHASENPRLP ESLAANKIVF IGPPGSAMRS LGDKISSTIV AQSAEVPTMA
WSGTGISETA MSEQGFVTVA DDVYKRACVT TVEEGMVRAE EIGYPVMIKA SEGGGGKGIR
KVEAPEQFKN AFSAVAGEIP GSPIFIMKLA GQARHLEVQL LADQYGNAIS LFGRDCSVQR
RHQKIIEEAP VTIAKQDIFE EMERAAVRLA KLVGYVSAGT VEYLYSHAED VFYFLELNPR
LQVEHPTTEM VSGVNLPAAQ LQVAMGIPLH RIRHIRQLYG VAPNGMSEID FEMVDPEASK
LQRKPRPKGH VVAVRITAEN PDAGFKPSSG SLQELNFRSS TNVWGYFSVG TAGGLHEFAD
SQFGHIFAYG EDRGESRKNM VVALKELSIR GDFRTTVEYL IKLLELQAFE ENTITTGWLD
SLISDKLTAE RPDATLAVIC GAVTKAHLAS EASWAEYKRI LDKGQAPSRD VLKTVFTIDF
IYDNVRYSFT ATRSSLTTWT LYLNGGRTLV GSRPLADGGL LVLLDGKSHS VYWREEVGAL
RLMIDSKTCS IEQENDPTQL RSPSPGKLVR YLVESGDHIN AGEAYAEIEV MKMYMPLTAS
EDGIVQFVKQ PGVSLDPGAI IGILTLDDPA RVKHAKPFEG LLPAMGPPNV IGNKPHQRLR
HYLNILNDIL DGFDNQAIMA STFKDLISVL ENPDLPFSEV SAILSALSGR ISSKLEDSIR
AAIETARGKG DATEFPAVRI KKLMEHFMED NIRAQDRPMF RTQLSALFDV VERYSNGLRG
HEVNTIAELL ARYEETEKLF GGSIEARVLA LREQYKDDLE KVAQLVLSHM MAQRKGRLVT
LILDHVKNSG STVSNPDSKL YQVLQGLASL EARSSTQVAL KAREVLISCQ MPSYEERKGQ
MQGILKASVT NSFYGEQGND VRQPSADVLR ELIDSRYTVY DVLPTFFNFH EQWVTFAALE
VYVRRAYRAY SLLSIDYEEG DGLDDGDAPH IVTWRFNLPQ SHSPPTTPSL ANVARRQASV
SDLTYMINKH QKQPLRTGAI ASFPNFAALT RGFDKVASTL PPFDVQEYRE RYGANNQPPN
VLNMALRIFK ETDDLSDSAW YEKAHELVNQ RSRVLAQRGV RRISILICRP GLYPQYFTLR
NMGSSWEEEQ AIRNVEPALA YQLELSRLSN YNLTPCFTES KQLHIYHAVA RENQLDSRFF
IRALVRPGRV RGDMNTAKYL ISETDRLVTN ILDTLEVVSA QHRNADVNHI FMNFIYNLPV
TYEDVLEAIA GFIERHGKRL WRLHVTGSEI RIVLEDNEGN VMPIRCIVEN VSGFIVNYHG
YQEITTDKGT TILKSIGEKG PLHLQPVHQP YPTKESLQPK RYQAHLIGTT YVYDFPDLFS
KALSNVWAKA RTLNNSCPLP KKVLESRELI LDENDQLQEV DRAPGNNTCG MVGWVFTLRT
PECPDGRRAV VIANDITYKI GSFGPEEDQF FYLVSQYARE QGLPRIYLSA NSGARIGLAE
EVMSLFSCAW NDPAHPEKGV DYLYLTHENF LKLQEKAASS ARTVEVEHGG ELRHKIVDII
GLQDGLGVEC LKGSGLIAGE TSRAYDDIFT ITLVTARSVG IGAYLVRLGE RAVQVEGQPI
ILTGAPALNK VLGREVYTSN LQLGGTQIMY KNGVSHLTAS SDLEGATHIL EWLSYVPEVK
GAPLPIVESA DPWDRDIGYS PPKGPYDPRW FIEGKTDETT SEWMPGFFDK GSFQETLSGW
AQTVVVGRAR LGGIPMGVIA VETRTVERLV PADPANPTSF EQRIMEAGQV WYPNSAYKTA
QAIFDFNREG LPLIIFANWR GFSGGQQDMY DEILKQGSKI VDGLSSYKQP VFVYIVPNGE
LRGGAWVVLD PSINSQQMEM YADVDSRAGV LEPEGIVEIK MRRDKILKLM ERLDSTYATL
KKDSTDSSKN ADERAAAMDA LAQRETLLQP TYKQIALLYA DLHDRVGRME AKGCAKSMVW
KDARRRFYWS VRAKIAWSAA MAELAEASPD SSTEYRTTLL ERLASVDSST ERRAVAEVLE
ALDLTAAVAQ LKADHLMRSM LALAHEDRKA TLDGLIRLVD NLTDDEKATL TGALQNSGRS
PGPPSYSNVS GTA
//
