ID A0A165HX05_9BASI Unreviewed; 2224 AA.
AC A0A165HX05;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetyl CoA carboxylase {ECO:0000313|EMBL:KZT59856.1};
GN ORFNames=CALCODRAFT_523153 {ECO:0000313|EMBL:KZT59856.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT59856.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT59856.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT59856.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV423936; KZT59856.1; -; Genomic_DNA.
DR STRING; 1353952.A0A165HX05; -.
DR InParanoid; A0A165HX05; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000076842; 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:UP000076842}.
FT DOMAIN 37..545
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 194..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 1463..1801
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1805..2121
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2224 AA; 247157 MW; AD4EB56B4C5075FB CRC64;
MASSTSNVAR FFGGNAVDKA VPGKVTDFVK SHGGHTVITK VLIANNGIAA VKEIRSVRQW
SYETFGTERA VEFTVMATPE DLKANAEYIR MADRYIEVPG GTNNNNYANV DVILDVAERA
GVHAVWAGWG HASENPRLPE SLHAHKNKIV FIGPPGSAMR SLGDKISSTI VAQHAEVPCM
PWSGTGISTT TLSDDGFVTV ADEVYNKACV KSVEEGLEKA KQIGFPVMIK ASEGGGGKGI
RKVEDAANFK NAFQAVMGEV PGSPIFIMKL AGSARHLEVQ LLADQYGNAI SLFGRDCSVQ
RRHQKIIEEA PVTIARPERF EQMEKAAVRL AKLVGYVSAG TVEYLYSHAE DSFFFLELNP
RLQVEHPTTE MVSGVNLPAA QLQIAMGIPL HRIRDIRTLY GVAPQGTSEI DFDMVNPQSA
LNQRKPMPKG HVVAVRITAE NPDAGFKPSG GHLQELNFRS NTNVWGYFSV GSTGGLHEFA
DSQFGHIFAY GADRSESRKN MVVALKELSI RGDFRTTVEY LIKLLETQAF EENTITTGWL
DTLISNKLTA ERPDATLAVI SGAVTKAHMA SEACWSEYRR ILDKGQVPAK DTIKTVFVID
FIYEGMRYSF TAARASQTLW TLYLNGGRTL VGARPLADGG LLVTLDGKSH SVYWREEVGA
LRLMIDAKTC LIEQENDPTQ LRSPSPGKLV RFLVDSGDHL KAGDAYAEIE VMKMYMPLIA
TEDGVPLFVK QPGVTLEPGD ILGILTLDDP ARVKHAKPFE GQLPPLGFPT VAGNRPHQRM
VHYMETLNNI LDGYDNQAVM QSTVKDLFEV LRDPELPFSE AASILASLSG RMPGKLEDAI
RASISQSKHR VGAEFPAARI KKLLESHMQE HVREQDRPMF RTQLGIVFDL CERYRNGLKS
HEWGTIATLL ERYENTSKLF GGRPETVVLK LRDEHKDNLD VVAGLVLSHS RAANKNKLVL
ALLDHVKEGG SRIANQEPKL YNVLKEIAGL ESKSCQPAAL KAREVLILTQ MPGYEERAIQ
MGDLLKNSVK TTYYGEAGDD TRTPAFETIK ELVDSRYTVY DVLPTFFEHD DQWVALAALE
VYIRRAYRAY EIMSVNYEEG DNLDDGDAPN VVTWKFRVGR SYSPPTTPRV ENGTVRRSGS
LSDFSYLLHK SQTEPARYGT IASFGDVAGA ERGFPKTAEL LPLPPRGETN QQNVVYIALR
VFSEADDMSD DKWMAAFLKM TNDNKDLIGS RGVRRVTFLI CRKGIYPWFY TLRYRDGNWE
EDEAIRNVEP ALAYQLELNR LSNFKLTPCF VENRQIHIYH AVARENQLDQ RFFVRALVRP
GRLRGPMRTR EYLISETDRL VGAILDSLEV VQPQFRNTDC NHIAINFVYN LHVTFEEVEE
ALAGFIERHG KRLWRLRVIG SEIRIVLEDE EGNVMPIRAV IENTTGFVVE YHSYQEVPSE
NGATVLKSIG QIGPLHLQLA KTPYTTKESL QPRRYQAHLV GTTYVYDYPD LFRQALKQVW
AKANKQNAKL IAPKDILDAK ELVMDEKGVL QPIARPPGSN VSGMVGWIFT LKTPEYPRGR
RVVVVSNDIT YKIGSFGPKE DDYFNAVTDL ARSLGLPRIY LSANSGARIG LAEEALSLFS
VAWNVPGNSD KGFKYLYLTP DNLSKLNEKA SGAVRTIEIE EDGEVRHKIT DIIGLQDGLG
VECLKGSGLI AGATSRAYDD IFTITLVSAR SVGIGAYLVR LGERSVQVEG QPIILTGSAA
LNKVLGREVY TSNLQLGGTQ IMYKNGVSHL TATNDLEGVQ HILEWMSYVP EAKGFPLPIR
PASDTWDREI GYMPPKAPYD PRWFIGGKTE EVDGSSEYLS GFFDDGSFQE TLGGWAQTVV
VGRARLGGLP MAVIAVETRT VERIIPADPA NPSSFEQRIM EAGQVWYPNS AYKTAQAIFD
FEREGLPLII FANWRGFSGG QQDMYDEILK QGSKIVDGLS AYTKPVFVYI MPNGELRGGA
WVVLDPSINP GQMEMYADVD SRGGVLEPEG VVEIKMRRDK ILSMMQRLDP EYARLAAVSK
DPTKSAEERV AAKDQLSLRE TELAPTYKQV ALLYADLHDR VGRMEAKGCA EPMEWKNARR
FFYWRLRARL ALASAFEQFK AVDSEMTDQS CEAMLLTAYP NLNFSDNRQL AEALENVDLA
QAVEKVQQLA VAREIKYLAA TNPTGAFSGL LAVLHTMTTE EKATLMAELQ SGETGMFKMP
GAYV
//
