ID A0A0D2E2I3_9EURO Unreviewed; 2291 AA.
AC A0A0D2E2I3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW49703.1};
GN ORFNames=PV05_11356 {ECO:0000313|EMBL:KIW49703.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49703.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49703.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49703.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847323; KIW49703.1; -; Genomic_DNA.
DR RefSeq; XP_013310287.1; XM_013454833.1.
DR STRING; 348802.A0A0D2E2I3; -.
DR GeneID; 25333264; -.
DR HOGENOM; CLU_000395_5_1_1; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000054342; 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:UP000054342}.
FT DOMAIN 62..570
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 219..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 1528..1867
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1871..2185
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2291 AA; 255578 MW; 36904D7987460680 CRC64;
MASTVNGVNG TPARRSTLVN GTTSEWQAKH NLAAHFIGGN RLEKAPPSKV KDFVQAHDGH
SVITSVLIAN NGIAAVKEIR SVRKWAYETF GDERAIQFTV MATPEDLQAN ADYIRMADQY
VEVPGGTNNN NYANVELIVD VAERMNVHAV WAGWGHASEN PKLPESLAAS PKKIIFIGPP
GSAMRSLGDK ISSTIVAQHA RVPCIPWSGE GVDEVELDDK GIVTVRDDVY DKGCVHSPQE
GLEAARKIGF PVMVKASEGG GGKGIRKVEN EEEFESLYNA AASEIPGSPI FIMKLAGNAR
HLEVQLLADQ YGNNISLFGR DCSVQRRHQK IIEEAPVTIA NPDTFRSMED AAVRLGELVG
YVSAGTVEYL YSHADDKFYF LELNPRLQVE HPTTEMVSGV NLPAAQLQIA MGIPLHRIRD
IRLLYGVDPH TATEIDFHFK DPASLKTQRR PRAKGHTTAC RITSEDPGEG FKPSSGTMHD
LNFRSSSNVW GYFSVSSASS IHSFSDSQFG HIFAYGENRQ ASRKHMVVAL KELSIRGDFR
TTIEYLIKLL ETPAFEDNTI TTGWLDQLIT NKLTAERPDP MLAVLAGALT KAHLASEACI
AEYRKGLEKG QVPSKDVLKT VFPVEFIYEG QRYKFTATRA SLDSYHIFIN GSKCSVGVRT
LADGGLLMLL AGRSHSIYWK EEATAIRISV DSKTCLLEQE NDPTQLRTPS PGKLVKYTVD
NGEHVKAGQA FAEVEVMKMY MPLIAQEDGV VQFLKQPGAT LEAGDILGIL ALDDPSRVKT
AETFTGKLPD LGPPQVVGNK PPQRFALLLG ILQNILLGFD NQVIMASTLK ELVSVLRDPE
LPYGEWAARS SALHSRTPQR LDSQLSQIVD RAHARHAEFP AKQLQKAINR FIEENMSKAD
GAILHTTLAP LEEVISRYAE GLKVHEFSVF TGLLEQYYEV EKLFASGSHR DEDVILKLRE
EHKDDILSVV YTVLSHTRVS SKNNLIVAIL AMYRPNQPNV GNVGKYFKPA LRHLTELESR
ATAKVALKAR ELLILCALPS LEERVSQMEH ILKSSVVESK YGEAGWEHRE PDLEILKEVV
DSRYTVFDVI PLFFAHHDPW VGLAALEVYI RRAYRAYTVR EVEYHNDVDP PFFMSWDFVL
RKVGQSEFGL PLASSYPSGQ ATPSQQGNGN AFKRIASVSD LSYLNKLQAE DEPTRKGVIA
PCHYLDEVDE CLSRALEVFP KGTKEKRPSQ QHLMPTLDSA RRPQQKAEPI DDDLTNVCNI
AIRDTEDLPD EEILGRVRSL VADYKSELLA RRVRRITFIC GHKDGSYPGY FTFRGPEYEE
DLTIRHNEPA LAFQLELGRL SKFKIKPVFT ENRNIHIYEA IGKGEDRDKV VDKRYFVRAV
VRPGRLKDEI PTAEYLISET DRLVNDICDA LEVIGNNNSD LNHIFINFSP VFNLQPKDVE
ETIAGFLERS ARRFLRLRVT GAEVRILCTD PETGMPYPLR VFITNTSGYV VNVESYVERK
SRSGDWVFET IGATNKVGAM HLRPVSTPYA TKEWLQPKRY KAHLMGTQYV YDFPELFRQA
IANSWTKAIA RHPPMAESRP ETGHCLEFSE LILDDNDELA EVSREPGTNN CGMVGWVLTA
KTPEYPRGRK FVIIANDITY QIGSFGPVED KFFNKCTEYA RKLGIPRVYL SANSGARIGM
ADELIPHFSV AWNDESKPEA GFKYLYLTPE KRKQLSAKEV MTEEIQEDGE TRHKITTIIG
AKDGLGVECL RGSGLIAGAT SKAYEDIFTI TLVTCRSVGI GAYLVRLGQR AIQIEGQPII
LTGAPALNKV LGKEVYTSNL QLGGTQIMYR NGVSHMTASD DFQGVEKIVE WMSFVPDKKG
QPVPVGIASD TWDRDIAFYP PRGPYDVRHL IAGKPDEEGF QSGLFDKDSF QEALGGWAKT
VVVGRARLGG IPMGVIAVET RTVENVIPAD PANADSMEQV VQEAGGVWFP NSAFKTAQAL
KDFNYGEQLP VMILANWRGF SGGQRDMFNE VLKYGSYIVD GLVKYEQPVF VYIPPFGELR
GGSWVVVDPT INPEQMEMYA DEESRGGVLE PEGIVGIKYR REKQLETMAR LDPIYGQLKA
QSLAKDSTPE QLNDIKAKMT EREQLLGPIY QQIALQFADL HDRAGRMEAK GTIRMPLKWQ
NARRFFYWRL RRKLSEEVLL KKLNSSLGAG TAVPTVSALA QKESNLAMLK NWSGLLDVEF
DKDDRKVAEW YESHRKEVYA KIDAVKGEAV AKKVSELLMG NKEGGLKGVR EVLSLVPTSE
REQLVKYLTG A
//
