ID X0I2S5_FUSOX Unreviewed; 2284 AA.
AC X0I2S5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EXL83138.1};
GN ORFNames=FOPG_04139 {ECO:0000313|EMBL:EXL83138.1};
OS Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL83138.1};
RN [1] {ECO:0000313|EMBL:EXL83138.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54008 {ECO:0000313|EMBL:EXL83138.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW808.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXL83138.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54008 {ECO:0000313|EMBL:EXL83138.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Annotation of Fusarium oxysporum PHW808.";
RL Submitted (MAY-2012) 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}.
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DR EMBL; JH658816; EXL83138.1; -; Genomic_DNA.
DR SMR; X0I2S5; -.
DR HOGENOM; CLU_000395_5_0_1; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000030676; 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}.
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 1523..1861
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1865..2180
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1222..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2284 AA; 255933 MW; 5C4A58CE0556988F CRC64;
MTEISAGAQE GANGRSVPYV NGKASYAEKF QIADHFIGGN RLENAPPSKV KDFVGQNDGH
TVITNVLIAN NGIAAVKEIR SVRKWAYETF GDERAIHFTV MATPEDLQAN AEYIRMADHY
VEVPGGTNNH NYANVELIVD IAERMNVHAV WAGWGHASEN PKLPESLAAS PNKIVFIGPP
GSAMRSLGDK ISSTIVAQHA EVPCIPWSGT GVDEVAVDDK GIVTVADDIY AKGCVTSWEE
GLERAKEIGF PVMIKASEGG GGKGIRKATE EEGFEALYKA AASEIPGSPI FIMKLAGNAR
HLEVQLLADQ YGNNISLFGR DCSVQRRHQK IIEEAPVTIA KPDTFKAMED AAVRLGKLVG
YVSAGTVEYL YSHADDKFYF LELNPRLQVE HPTTEMVSGV NLPAAQLQIA MGIPLHRIRD
IRLLYGVDPK TSSEIDFEFK NEGTSMSQRR PQPKGHTTAC RITSEDPGEG FKPSNGVMHE
LNFRSSSNVW GYFSVGSQGG IHSFSDSQFG HIFAYGENRS ASRKHMVMAL KELSIRGDFR
TTIEYLIKLL ETEAFEDNTI STGWLDELIS KRLTAERPET MLAVVCGAVT KAHIASEACM
AEYRAGLEKG QVPSKDVLKT VFTIDFIYEG YRYKFTATRA SVDSYHLFIN GSKCSIGVRS
LSDGGLLVLL DGRSHNVYWK EEVGATRLSV DSKTCLLEQE NDPTQLRSPS PGKLVKYSVE
NGAHVRAGQA FAEVEVMKMY MPLVAQEDGV VQLIKQPGAT LEAGDILGIL ALDDPSRVKQ
AQAFVDKLPA YGEPVVVGAK PAQRFSLLYN ILHNILLGYD NSVIMANTLK ELIEVLRDPE
LPYSEWNAQF SALHSRMPQK LDAQFTQIVE RSKSRHGEFP AKALTKAFNK FLEDNVDAGD
AELLKGTLSP LTEVLDMYAE GQKNRELNVI KGLLEQYWEV ENLFMNQPQE DAVILQLRDQ
HKEDIMKVVH TVLSHSRVSS KSSLILAILE EYRPNKPKAG SIAKNLRETL RLLTELQSRP
TSKVSLKARE IMIQCALPSL EERTAQMEHI LRSSVIESRY GETGWDHREP SLDIIKEVVD
SKYTVFDVLT MFFAHDDPWV SLASLEVYVR RAYRAYILKQ IEYHQDENDA PQFVSWDFQL
RKLGQSEFGL PLQSAAPSTP ATPSGGEFNF KRIHSISDMS YLTGKWEDEP TRKGVIVPCK
YIDDAEDLIA KALEALALEQ KQKKKNTPGT PGLIPDLSGK RKPAQPKQHE EELSAVINVA
IRDLESRDDR EALEDILPIV EQFKDELLAR GVRRLTFICG HSDGSYPGYY TFRGPEYKED
DSIRHSEPAL AFQLELARLS KFHIKPVFTE NKSIHVYEGI GKNVDTDKRY FTRAVIRPGR
LRDEIPTAEY LISEADRVVN DIFDALEIIG NNNSDLNQVF INFSPVFQLQ PKEVEESLQG
FLDRFGIRAW RLRIAQVEIR IICTDPQTGE PYPLRVVITN TSGYVVDVDM YAERKSEKGE
WVFHSIGGTH EKGPMHLMPV STPYATKNWL QPKRYKAHLM GTQYVYDFPE LFRQAIQNSW
VKAVKAQPSL ASQQPKTGDC ISFTELVLDD KDSLDEVNRE PGTNTCGMVG WIFRARTPEY
PNGRRFIVIA NDITYKIGSF GPKEDDFFHK CTELARKLGI PRIYLSANSG ARLGLADELM
GHFKVAWNNP EKQDSGFKYL YLDEETKTRF EKDVITEEVS EDGEKRHKIV TIVGKEDGLG
VECLRGSGLI AGATSRAYND IFTVTLVTCR SVGIGAYLVR LGQRAVQIEG QPIILTGAPA
LNNLLGREVY TSNLQLGGTQ IMYRNGVSHM TANDDFAGVS KIVEWMSFVP EKRNSPVPVS
PSVDDWNRDI TYFPPQKQPY DVRWMISGRE GENGFESGLF DKDSFVEALG GWAKTVVVGR
ARLGGIPMGV IAVEVRSVEN ITPADPANPD SIEQVSNEAG GVWYPNSAFK TAQAINDFNN
GEQLPLMILA NWRGFSGGQR DMYNEVLKYG SFIVDALVKY EQPIFIYIPP FGELRGGSWV
VVDPTINSTA MEMYADTEAR GGVLEPEGII GIKYRKDKQV QTMARMDPTY AGLKKQLEDS
SLSTEETDEI KKKMAIREKQ LLPVYAQIAV QFADLHDRAG RMKAKGVIRD VLEWTNARRF
FYWRLRRRLN EEYILRRMTS TIISTSHSQT ATKNTETRDR YLHLLRSWSG IVDWEKNDQA
VTEWYETERK TISEKVETLK SEVLAAEVAS VVRGHAKAGW TGVREVLRVM PVEEREQILK
YLQQ
//
