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Database: UniProt
Entry: A0A0M8P6G4_9EURO
LinkDB: A0A0M8P6G4_9EURO
Original site: A0A0M8P6G4_9EURO 
ID   A0A0M8P6G4_9EURO        Unreviewed;      2273 AA.
AC   A0A0M8P6G4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KOS42274.1};
GN   ORFNames=ACN38_g6855 {ECO:0000313|EMBL:KOS42274.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS42274.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS42274.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS42274.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-2015) 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:KOS42274.1}.
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DR   EMBL; LHQQ01000110; KOS42274.1; -; Genomic_DNA.
DR   STRING; 229535.A0A0M8P6G4; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000037696; 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:UP000037696}.
FT   DOMAIN          46..554
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          198..395
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          681..755
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1506..1848
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1852..2167
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2273 AA;  253452 MW;  06D45830B27E858A CRC64;
     MGITNGNGAT IAKQDLPSHF IGGNALESAP PSAVKDFVTA HDGHSVITSV LIANNGIAAV
     KEIRSVRKWA YETFGNERAI QFTVMATPED LTANADYIRM ADQYVEVPGG TNNNNYANVE
     LIVDIAERMD VHAVWAGWGH ASENPRLPES LAASPKKIIF IGPPASAMRS LGDKISSTIV
     AQHAGVPCIP WSGTGVDAVK LDEHGIVTVE DEVYKQGCTF SPEEGLAKAK EIGFPVMVKA
     SEGGGGKGIR KVENEEEFHA LYNAAANEIP GSPIFIMKLA GNARHLEVQL LADQYGNNIS
     LFGRDCSVQR RHQKIIEEAP VTIAKQPTFQ AMERAAVSLG RLVGYVSAGT VEYLYSHSDD
     KFYFLELNPR LQVEHPTTEM VSGVNLPAAQ LQIAMGIPLH RVRDIRLLYG VDANASADID
     FDFSNEESFQ TQRRPQPKGH TTACRITSED PGEGFKPSSG TMHELNFRSS SNVWGYFSVG
     TAGGIHSFSD SQFGHIFAYG ENRSASRKHM VVALKELSIR GDFRTTVEYL IKLLETPAFE
     DNTITTGWLD QLITNKLTAE RPDQTVAIIC GAVTKAHLAS EAGIEEYRHG LGKGQVPSKE
     ILKTVFPVDF IYEGERYKFT ATRASLDSYH LFINGSKCSV GVRALADGGL LVLLSGRSHN
     VYWKEEAAAT RLSVDGKTCL LEQENDPTQL RSPSPGKLVK FTVENGEHIR SGQSYAEVEV
     MKMYMPLIAK EDGIVQLIKQ PGATLEAGDI LGILALDDPS RVKHAQPFTG QLPELGSPTV
     LGNKPSQRFF LLHSILENIL RGFDNQVIMG TTLKDLVEVL RNPDLPYGEW NAQSSALHSR
     IPQRLDAQLQ NVVDRAKTRK AEFPAKQLQK AIVRFIEENI GPADAEILKG TLLPLVQVIN
     KYLDGLKSNE YNVFIGLLEQ YYDVEKLFST HNLRDEDVIL KLREENKDDI TSIVHTVLSH
     SRIGSKNNLV LAILDMYRPN QPLLENVGTH FKPILKKLTE LEARSSAKVT LKAREVLIQC
     AMPSLDERLS QMEHILRSSV VDSRYGETGW EHREPSLEVL KEVVDSKYTV FDVLPRFFVH
     ADPWVTIASL EVYVRRAYRA YTLKGIEYHA STEQPFMSWD FTLGKLGHRE FGVLNSTQPS
     APGTPVAEIN PFKRINSIGD MSLFVSDAAS DPVRKGVIIP VQYLEDAEES LSKALEVFPV
     GGSNAKRPSE QGLIASLEGK RRPATKPVSD SELTGVCNIA IRDIEDMEDS EIVEQMKQLL
     ADNKDELLAR RIRRVTFICG KQGVYPGYFT FRGPNYEEDL SIRHSEPALA FQLELGRLSK
     FNIKPVFTEN RNIHVYEAMG KGPENDKAID KRYFIRAVVR PGRLRDDIPT AEYLISEADR
     LMNDILDALE IIGNNNSDLN HIFINFSPVF NLQPVDVEQA LAGFLDRFGR RLWRLRVTGA
     EIRILCTDPA TGMPYPLRVI ISNTYGFIIN VELYIERKSE KGEWIFQSIG GTAKLGSMHL
     RPVATPYPTK EWLQPKRYKA HLMGTQYVYD FPELFRQAFQ NSWTKIAEKI PSLYEKRPPV
     GECIDYSELV LDDTDNLVEV SREPGTNTHG MVGWIITART PEYPRGRRFI IVANDITFQI
     GSFGPQEDKF FHKCTELARK LGIPRIYLSA NSGARIGVAD EIIPYFSVAW NNPEKPEAGF
     KYLYLTPEVK KRFDASKKKE VITELINDEG EERHKITTVI GAKDGLGVEC LKGSGLIAGA
     TSKAYEDIFT ITLVTCRSVG IGAYLVRLGQ RAIQVEGQPI ILTGAPAINK LLGREVYTSN
     LQLGGTQIMY KNGVSHMTAT DDFEGVEKIV EWMSFVPDKK NAPIPIRPWS DNWDRDVAYF
     PPPKQPYDVR YLIGGKEDVD GFLPGLFDKG SFEEALGGWA RTVVVGRARL GGIPMGVIAV
     ETRSVENVTP ADPANPDSME MISTEAGGVW YPNSAYKTAQ ALRDFNNGEQ LPVMILANWR
     GFSGGQRDMY NEVLKYGSYI VDALVKYEQP IFVYIPPHGE LRGGSWVVVD PTINPDQMEM
     YADEESRGGV LEPEGMVNIK YRRDKQLDTM ARLDATYGEL RRSLADTSLT NEQLTEVKAK
     MATREEQLLP VYMQIALQFA DLHDRAGRMQ AKNTIRKPLQ WVNSRRFFYW RLRRRLSEET
     IVKRMVAASA PPAPGADAFG QSLRATHLRT LHAWTGLLDE ELEHDDHKVA TWYEENKKVV
     QSKVESLRTD GVASEVAQLL IGNKEGGLRG VQQVLSMLPV EERENVLKYL GSA
//
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