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Database: UniProt
Entry: A0A1B8ABF3_FUSPO
LinkDB: A0A1B8ABF3_FUSPO
Original site: A0A1B8ABF3_FUSPO 
ID   A0A1B8ABF3_FUSPO        Unreviewed;      2280 AA.
AC   A0A1B8ABF3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OBS17794.1};
GN   ORFNames=FPOA_09526 {ECO:0000313|EMBL:OBS17794.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS17794.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS17794.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS17794.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBS17794.1}.
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DR   EMBL; LYXU01000004; OBS17794.1; -; Genomic_DNA.
DR   STRING; 36050.A0A1B8ABF3; -.
DR   OMA; PTPKGHC; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000091967; 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:UP000091967}.
FT   DOMAIN          62..570
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          220..411
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          697..771
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1520..1858
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1862..2177
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          1219..1242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2280 AA;  255394 MW;  117EC956C6D7AB56 CRC64;
     MTEISAGAQE GANGRSVPYV NGKQSYAEKF NIADHFIGGN RLANAPPSKV KDFVGQNDGH
     TVITNVLIAN NGIAAVKEIR SVRKWAYETF GDERAIHFTV MATPEDLQAN AEYIRMADHY
     VEVPGGTNNH NYANVELIVD IAERMNVHAV WAGWGHASEN PKLPESLAAS PNKIVFIGPP
     GSAMRSLGDK ISSTIVAQHA AVPCIPWSGT GVDQVAVDDK GIVTVADDIY AKGCVTSWEE
     GLEKAKEIGF PVMIKASEGG GGKGIRKATE EEGFEALYKA AASEIPGSPI FIMKLAGNAR
     HLEVQLLADQ YGNNISLFGR DCSVQRRHQK IIEEAPVTIA KADTFKAMED AAVRLGKLVG
     YVSAGTVEYL YSHADDKFYF LELNPRLQVE HPTTEMVSGV NLPAAQLQIA MGIPLHRIRD
     IRLLYGVDPK TSSDIDFEFK NEETASSQRR PQPKGHTTAC RITSEDPGEG FKPSNGVMHE
     LNFRSSSNVW GYFSVSSQGG IHSFSDSQFG HIFAYGENRS ASRKHMVMAL KELSIRGDFR
     TTIEYLIKLL ETEAFEDNTI STGWLDELIS KRLTAERPET MLAVTCGAVT KAHIASEACM
     TEYRAGLEKG QVPSKDVLKT VFTIDFIYEG FRYKFTATRA SVDSYHLFIN GSKCHVGVRS
     LSDGGILVLL DGRSHSVYWK EEVGATRLSV DSKTCLLEQE NDPTQLRSPS PGKLVKYSVE
     NGAHVRAGQA FAEVEVMKMY MPLLAQEDGV VQLIKQPGAT LEAGDILGIL ALDDPSRVKQ
     AQAFVDKLPA YGEPVVVGAK PAQRFSLLYN TLQNILLGYD NSVIMASTLK ELIEVLRDTE
     LPYSEWNAQF SALHSRMPQK LDAQFTQIIE RGKSRNSDFP AKALSKAFHK FIEDNVDAND
     AGLLKTTLAP LTEIIDMYID GQKNRELTVI KSILEQYYEV EALFMNQPQE DAVILQLRDQ
     NKDDIMKVVH TVLSHSRVSS KSSLILAILE EYRPNKPKAG NVAKNLRETL RLLTELQSRH
     TSKVSLKARE IMIQCALPSL EERTSQMEHI LRSSVVESRY GETGWDHREP SLDIIKEVVD
     SKYTVFDVLT MFFAHDDPWV SLASLEVYVR RAYRAYLLKQ IEYHQDENDN PQFVSWDFQL
     RKLGQSEFGL PLQSAAPSTP ATPSGGEFNF KRIHSISDMS YLSSKWEDEP TRKGVIVPCK
     YIDEAEDLIG KALEALAHEQ KQKKKNTPGL IPDLSGKRKP APLKQSEEEL SAVINVAIRD
     VESRDDREAL EDILPIVEQY KDELLARGVR RLTFICGHSD GSYPGYYTFR GPEYKEDDSI
     RHSEPALAFQ LELARLSKFN IKPVFTENKS IHVYEGIGKK HDTDKRYFTR AVIRPGRLRD
     EIPTAEYLIS EADRVVNDIF DALEIIGNNN SDLNHVFINF SPVFQLQPKE VEESLQGFLD
     RFGIRAWRLR IAQVEIRIIC TDPQTGEPYP LRVVITNTSG YVVDVDMYAE RKSEKGEWVF
     HSIGGTHEKG PMHLMPVSTP YAIKNWLQPK RHDAHGMGTQ YVYDFPELFR QAIQNTWNKA
     VKAQPSLASQ QPKTGDCISF TELVLDDKDN LDEVNREPGT NTCGMVGWIF RARTPEYPNG
     RRFIVIANDI TYKIGSFGPK EDEFFHKCTE LARKLGIPRI YLSANSGARL GLADELMGHY
     KVAWNNPEKQ DAGFKYLYLD DAAKTRFEKD VITEEVTEDG EKRHKIVTII GKEEGLGVEC
     LRGSGLIAGA TSRAYNDIFT VTLVTCRSVG IGAYLVRLGQ RAVQIEGQPI ILTGAAALNN
     LLGREVYTSN LQLGGTQIMH RNGVSHMTAN DDFAGVSKIV EWMSFVPEKR NSPVPVSPSV
     DDWNRDVTYY PPQKQPYDVR WLIGGREGEN GFESGLFDKD SFVEALGGWA KTVVVGRARL
     GGIPMGVIGV EVRSVENITP ADPANPDSIE QVSNEAGGVW YPNSAFKTAQ AINDFNNGEQ
     LPLMILANWR GFSGGQRDMY NEVLKYGSFI VDALVKYEQP IFIYIPPFGE LRGGSWVVVD
     PTINPTAMEM YADTEARGGV LEPEGMIGIK YRKQKQIQTI IRMDPTYAGL KKQLEDSSLS
     TEQTDEIKKK MAAREKELLP VYSQIALQFA DLHDRAGRMK AKGVIRDVLE WSESRRFFYW
     RLRRRLNEEY ILRRMTSTII STSHQAAAKD KETRDKYLHL LRSWSAIVDW ETNDQAVTEW
     YETERKTISE KVEALKSEVL AAEVANVVRG HAKAGWTGVR EVMRVMPVEE REQLLKYLQQ
//
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