ID A0A166FAN4_9AGAM Unreviewed; 2233 AA.
AC A0A166FAN4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acetyl CoA carboxylase {ECO:0000313|EMBL:KZP16603.1};
GN ORFNames=FIBSPDRAFT_1047401 {ECO:0000313|EMBL:KZP16603.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP16603.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP16603.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP16603.1,
RC ECO:0000313|Proteomes:UP000076532};
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; KV417591; KZP16603.1; -; Genomic_DNA.
DR STRING; 436010.A0A166FAN4; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000076532; 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 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:UP000076532}.
FT DOMAIN 37..545
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 189..386
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 672..746
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1472..1810
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1814..2128
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; 248409 MW; BA02730830124960 CRC64;
MAYDHSKVTN YIGGNDLDKA PEGRVTDFVR EHGGHTVITK VLIANNGIAA VKEIRSIRQW
SYETFGTERA VEFTVMATPE DLKVNAEYIR MADRYIEVPG GSNNNNYANV DLIVDIAERM
GVHAVWAGWG HASENPRLPE SLAASKHKIV FIGPPGSAMR SLGDKISSTI VAQHAKVPTM
PWSGTGITDT TLSESGYVTV PDKAYHEACV TSVEDGLVKA EKIGWPVMIK ASEGGGGKGI
RMVAEPEAFK NAYHAVAGEI PGSPIFIMKL AGQARHLEVQ LLADQYGNAI SLFGRDCSVQ
RRHQKIIEEA PVTIAKEETF AQMERAAVRL AKLVGYVSAG TVEYLYNHAE DDFYFLELNP
RLQVEHPTTE MVSGVNLPAA QLQIAMGIPL HRIRHIRQLY GVAHTGTSEI DFDMSTAESK
ELQRKPRPKG HVVAVRITAE NPDAGFKPSS GSIQELNFRS STNVWGYFSV STSGGLHEFA
DSQFGHIFAY GEDRGESRKN MIVALKELSI RGDFRTTVEY LIKLLELEAF RENTITTGWL
DSLISNKLTA ERPDTSLAVI SGAVTKAYLA SEECWNEYKR ILDKGQVPAR DVLKTVFGID
FIYENVRYSF TAARSSWTTW TLYLNGGRTM VGARPLADGG LLVLLDGKSH SVYWREEVGA
LRVMVDAKTC LIEQENDPTQ LRSPSPGKLI RFFVDSGEHI NAGEQYAEIE VMKMYMPLVA
SEDGIVQFVK QPGVSLEPGD ILGILTLDDP ARVKHAKPFE GLLPSLGSPG VTGGKPHQRF
TSSLGILNDI LDGFDNQAVM TSTFKDFTEV LHDPELPYSE VTAILSSLSG RMPQKLEDGV
RQAIETAKSK TDSLHEFPAV RIKKVLEHYI KESVLPADIT MFRSKLGDLF DVLERFAGGL
KGFETDTIAN LLTHYEGTEK LFGGSIEARV LALREQHKDD LDKVVGLVLS HIKAQSKVKL
VLLILDYVKT SGLPVANSES RLYKVLQSLA VLEAKSSTPV TLKAREVLIA GQMPSYEERL
GQMEIVLKNS ISKNYYGEAG ASDKTPSAEI LKELSDSQYT VFDVLPAFFN HKDHLIVLAS
FEVYVRRAYR AYSLLSLDYE EGDGLDDGEL PHIVTWRFNL GQSHSPPMTP RIDVAPRRQG
SVSDLTYMIN KSQTQPIRTG ALASFPNLDA LAIGFDKVAS MLPVFEPEEY RRRYGANNQP
PNIMNLALRI FDEEDDMPDA EWSEKVITLV NERKASLNKR GVRRVSVLIC RRTEYPYYYT
LRETNGVWGE EQALRNIEPA LAFQLELSRL SNYKLTPCFG ESQQIHIYQA NARENQLDNR
FFIRALVRPG RLRGTMSTAE YLISETDRLV TGVLDALEVV SAKHRNADCN HIFMNFVYNL
NVTYEDVLEA ISGFIERHGK RLWRLHVSGS EIRIALEDSE GNVTPIRCII ENVSGFVVNY
HGYQEITTDK GTTILKSIGE KGPLHLQPVN AAYPTKESLQ PKRYQAHLIG TTYVYDFPDL
FSKALNNSWN SARDTDPSLV LPKKFLESKE LVLDENDKLA EVDRAPGNNT FGMVGWVFTM
RTPEYPKGRK VVVIANDITY KIGSFGPVED NFFYLATQYA RDHGLPRIYL SANSGARIGL
AEETLGLFSV AWKEQDKPEK GIDYLYLTRE NYLTLQDKGP DAVRIAEIEV DGEQRYQITD
IIGLQDGLGV ESLKGSGLIA GETSRAYDDI FTITLVTARS VGIGAYLVRL GERAVQVEGQ
PIILTGAPAL NKVLGREVYT SNLQLGGTQI MHKNGVSHLT AASDLEGATH ILDWISYVPA
VKGDPLPVRE TTDSWDRDIT YTPPKGAYDP RWFITGKEDE QSSEWQSGFF DKGSFQETLS
GWAQTVVVGR ARLGGIPMGV IAVETRTIER IVPADPANAA SFEQRIMEAG QVWYPNSAYK
TAQAIFDFNR EGLPLIVFAN WRGFSGGQQD MYDEVLKQGS KIVDGLSSYK QPVFVYIVPN
GELRGGAWVV LDPSINPEQM EMYADVDARG GVLEPEGIVE IKMRRDKILT LMDRLDTTYA
THKRDSKDAT KTEEERAKAT QDLAAREQFL QPSYKAMALL YADLHDRVGR MEAKGCAKPA
VWKDARRKFY WAVRARVSRS YLLAELAEAS PESTPEYRSR LLNSLAFVDA KTDPRVASEA
LEKLDISSTV AQLKSDYLLR RLIDTAQQDR KGVLASLIRL ADNLSDEDRS SLVTALSNKD
RSPGPPSYTN AAK
//
