ID A0A316Z0S3_9BASI Unreviewed; 2161 AA.
AC A0A316Z0S3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:PWN93715.1};
GN ORFNames=FA10DRAFT_264325 {ECO:0000313|EMBL:PWN93715.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN93715.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN93715.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN93715.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819634; PWN93715.1; -; Genomic_DNA.
DR STRING; 215250.A0A316Z0S3; -.
DR InParanoid; A0A316Z0S3; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000245768; 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; 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; 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:UP000245768}.
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 676..750
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1452..1786
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1790..2088
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2161 AA; 237479 MW; 8862AE9D50CC531D CRC64;
MPLADHQKVS HFIGGNSLEA APAGTVADFV RKSQGHTVIT KVLICNNGIA AVKEIRSIRK
WSYETFGDER AIEFIVMATP EDLKVNADYI RMADQYVEVP GGTNNNNYAN VDLIVDVAER
TGVHAVWAGW GHASENPRLP ETLAASKQKI IFIGPPGSAM RSLGDKISST IVAQHADVPC
MPWSGTGIKE TMMSEQGFLT VSDEVYQKAC IHSAEEGLEK AEIIGFPVMI KASEGGGGKG
IRMCGSAPDF RQLYNAVLGE VPGSPVFVMK LAGKARHLEV QLMADQYGNA ISIFGRDCSV
QRRHQKIIEE APVTIAPDAA REEMERAAVR LAKLVGYVSA GTVEWLYSPE NDSFSFLELN
PRLQVEHPTT EMVSGVNIPA AQLQVAMGIP LYRIRDIRTL YGMDPRGAEM IDFDFEDPAS
LQKQRKPQPK GHVIACRITS ENPETGFKPG MGALSDLNFR SSTSTWGYFS VGQSGALHEF
ADSQFGHVFA YGLSRQEARQ NMVVSLKELS IRGDFRTIVE YLIMLLEKPA FEQNQFSTAW
LDGLIKDRVS SDKPPLQIAV ICGAVVKAHL RSQECEALYM SILNKGQVPP RDTVKTTFSG
ITFIIDGVKY SVTCSRSSAS GWTVYLNGAR TQVATRSLTD GGMLIGLSGR SHPTYWREEA
GGASLRLMVD SRTALLEEET DPSQIRSPSP GKLVSLLVPS GSHVEAGQAI AELEVMKMYM
PLTTAESGVV NFLASPGTPV AAGDHLAILS LDDPSKVMRA KPFDGQLPDA GLPIVIGSKP
HQRFQYVLSV LNDVLDGFDQ SVQMQACLTE LVELLNNVET PYGQALQALS SLSGRVPSRL
EELLRTTIDA AQGKGQEFPA ARLRKLIDNY IRDSVDPAVR LQVQTTLTPL TTLFEEYAPG
LKQHSANVLA GLLEKYYDVE SPFTGEADVI LTMRQEADSL DKVVAQQISH NGVLLKNALV
ISILNQDTVK RSAGLSDATK VNVALQKLAS LEGKATAPVA LKAREVSISR DLPSLKDRKR
QMESILKASV MSSIYGGDSE YHEPSLNTLR ELSDSQYTVY DVLHSFFDSS VPSHVAFAAL
VTYVLRAYRA YDVVNFDYAV EDFDADERAV LKWQFRLLAS RQQAERQASD GDLVAQGKKS
DANNVQSGLR QGVMTSCATF EDLGDVIPRA LRFFDKSPPT NIVNIAVTGE ASTTDVEARG
EFVKWTNKFA DQLEAAGVRR ITFLHCQPGI YPWFTTLRAG PSQWTEEKAI RNIEPALAYQ
LELDRMTTNF DITPVPVSSS TIHLYFARGI ANPADTRFFV RSLVRPGRIQ TGNQAEYIIS
ASDRIVNDIL NTLEVAMAQP EYRNADASHI FMSFIYQLDI TIDDVQKALA GFIDRHGLRL
FRLRITAAEI RLVLKGKREP QQIRAFITNE TGLVVRYEAY EEVAAQDGSV LLSNIAGPSA
PAPLHMQSAH APYATKVALQ SRRSRAHALQ TTFCYDFIDV LRQSLRANWK KAASKHPSDP
IRSLQELVFD EKESLRPVKR APGMNKIGMV AWLVDLLTPE YPAGRQIIVI ANDVTIQAGS
FGPAEDRFFA AASRMARQMG IPRLYISANS GARIGLATEV MDLFKAKFVD DDPVKGFQYL
YLDQQGYDAL EAKASGSVYT QQTKAEDGSV HHVITDIIGL QDGLGVECLS GSGLIAGETS
RAKEEIFTTT IVTGRSVGIG AYLARLGERV IQVEGSPMIL TGYQALNKLL GREVYTSNLQ
LGGPQIMYRN GVSHLVAKDD LAAMTSFVRW LSFVPSTRHA ALPKLVSSDS WDRTVGFAPP
AGPYDPRCLI EGQADVTGLF DKGSWQETLG GWATSVVVGR ARLGGIPIGV IAVETRTLER
VLPADPANPN SQEQRIMEAG QVWYPNSAYK TAQAIVDFNR EGLPLMILAN WRGFSGGQED
MFQQILKYGS MIVDGLSAYR RPVFVYLPPK AELRGGAWVV VDRTINENGM MEMYADPSSR
GGVLEPEGIV SVKYRQDKQR ETMRRLDPVY AKLAAQEDRR GMAEREKAIA PIFSSVAVAY
ADLHDRTGRM SAVGVIRQAV EWKEARRFFY QRLQRRLVEE AALDSISTTD KNEARTVLEE
ILGVGLDDAD DATMAKLIQD KSKALAQIVQ ERQRQAAADQ ITQLAATLDP ETRKVLLASL
Q
//
