ID A0A072P7Z4_9EURO Unreviewed; 1135 AA.
AC A0A072P7Z4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE RecName: Full=Acetyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O9_08583 {ECO:0000313|EMBL:KEF55832.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF55832.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF55832.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF55832.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KEF55832.1}.
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DR EMBL; AMGV01000007; KEF55832.1; -; Genomic_DNA.
DR RefSeq; XP_013258422.1; XM_013402968.1.
DR AlphaFoldDB; A0A072P7Z4; -.
DR STRING; 1182545.A0A072P7Z4; -.
DR GeneID; 25283495; -.
DR VEuPathDB; FungiDB:A1O9_08583; -.
DR HOGENOM; CLU_009218_0_0_1; -.
DR OrthoDB; 196847at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR051602; ACC_Biotin_Carboxylase.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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; 2.
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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT DOMAIN 5..466
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..330
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 504..575
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 873..1129
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 573..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1060..1087
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 574..585
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 122836 MW; C7882A88ECAF4FA8 CRC64;
MSSSQPIKIL IANRSEIACR LIRTYSLYSN IHTVALFTPS EKEATHVRLA TASVALPGEG
PRAYLDAANI VSIAKKEGCW GIAPGYGFLS EDAGLVRLCE DEGIMFIGPS SEQLAQLGNK
MSARSLAVGA GIPVLDGTKT ALDRGSSITD VLSFGKSLGP ASKVILKAAA GGGGRGIRII
DDNTDEQAIR LAYEACQREA HASFGNESLF AERYLHGAKH IEVQLLGDGT GEVCHFWERE
CSLQRRNQKV VEIAPSHSIT PRLRRAIIEA AMKLGKAVKL RSLATIEFLV DAATEDYYFM
EANPRIQVEH TITEQINGID LVDLQLQVAL GRTLADLHIT REPPPPRLTS IQLRINAESF
RQDGTAQPEA GIIRQGHFPT GAGVRVETAL EGGRQYAVSP LFDSLLAKLI ATSSSYESAL
RLARWVIDKT RIVGCRTNQA FLMALLDFQT VQEGKCNILT IEENFETLYR ATQQFEEVLR
AKGDRISEEA TSLREDGAKS ERPAGSEELP ALVTGVVLSI KVSGGDKITA GQELLVLEAM
KMEHSVRSAY NGVVVKVAVT QGQQVTAGDP LIFTSSDGDN SSTNTHDLAE TESPEKLRPE
LTELNERQAF LRYAGREEDV AKRHANGYLT GRENLDLLVD KDSFIEYGDL VVAAQRKRYP
MSHLIARTSG DGIIVGWAKI DSHPVAVVIG DYLVLAGTQG HFHHQKLDRI FQSIIDHPAP
LVLYAEGGGG RPGDTDHLGM AGLKTPSFAL MGEIKARGIP SVAVVNGYCF AGNAAFLGTC
DIIIATRGGS TDAPLGKSTT IGMGGQAMIE GGGLGRFEHE HIGPVDVHMR SGGIDVLVDT
EVEAAPLVRK ILALFTHPQL PPAKSPYTSD PLLLRTAVPP LSSRRRAYDV RRVINLFLDD
DSFIEFCPEW GLSVLTGFGR INGHAVAIMA SNSSSPLGGA IDVASGAKVN RLLRLLTRLG
GMHLLSLCDT PGFMVGPDFE RSNEAQGTGS TYRCFGDWFG NSQEFTLLGG RVLGVVLRNG
FGLGAQAMLG GGSLNNSMCV AWPSAVFGGM GIEGAVRLAY KKELEAINDL EERKKREQEM
IDVMYSEGKA LNMAMATEID SVIDPATTRK WLEQMIEVLP KRVPTYVKAR RRAKM
//
