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Database: UniProt
Entry: A0A059BL04_EUCGR
LinkDB: A0A059BL04_EUCGR
Original site: A0A059BL04_EUCGR 
ID   A0A059BL04_EUCGR        Unreviewed;      2265 AA.
AC   A0A059BL04;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW66724.1};
GN   ORFNames=EUGRSUZ_F00484 {ECO:0000313|EMBL:KCW66724.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW66724.1};
RN   [1] {ECO:0000313|EMBL:KCW66724.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW66724.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) 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; KK198758; KCW66724.1; -; Genomic_DNA.
DR   RefSeq; XP_010060156.1; XM_010061854.2.
DR   STRING; 71139.A0A059BL04; -.
DR   EnsemblPlants; KCW66724; KCW66724; EUGRSUZ_F00484.
DR   GeneID; 104448070; -.
DR   Gramene; KCW66724; KCW66724; EUGRSUZ_F00484.
DR   KEGG; egr:104448070; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   InParanoid; A0A059BL04; -.
DR   OMA; PTPKGHC; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
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; 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          47..554
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          200..394
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          1502..1841
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1845..2160
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2265 AA;  252532 MW;  5B2925A7EAA66D75 CRC64;
     MAAAQRKPSL TSLGRVNGYT NGVLPVRSPA TVSAVDEFCK ALGGKRPIHS ILISNNGMAA
     VKFMRSVRTW AYETFGTEKA ILLVAMATPE DMRINAEHIR IADQFVEVPG GTNNNNYANV
     QLIVEMAEIT HVDAVWPGWG HASENPELPD ALNAKGIVFL GPPAISMAAL GDKIGSSLIA
     QAADVPTLPW SGSHVKMSPD SCLVTIPDEI YREACVYTTD EAIASCQVVG YPAMIKASWG
     GGGKGIRKVH NDDEVRALFK QVQGEVPGSP IFIMKVASQS RHLEVQLLCD QYGNVAALHS
     RDCSIQRRHQ KIIEEGPITV APIETVKKLE QAARRLAKSV NYVGAATVEY LFSMDTGEYY
     FLELNPRLQV EHPVTEWIAE VNLPAAQVAV GMGIPLWQIP EIRRFYGMEH GGNYDAWRRT
     SVVATPFDFD KAESTRPKGH CVAVRVTSED PDDGFKPTSG KVQELSFKSK PNVWAYFSVK
     SGGGIHEFSD SQFGHVFAFG ESRALAIANM VLGLKEIQIR GEIRTNVDYT IDLLHALDYR
     DNKIHTGWLD SRIAMRVRAE RPPWYLSVVG GALYKASASS AAVVSDYIGY LEKGQIPPKH
     ISLVNSQVSL NIEGSKYTID MVRGGPGSYR LKMNESEVEA EIHTLRDGGL LMQLDGNSHV
     IYAEEEAAGT RLLIDGRTCL LQNDHDPSKL VAETPCKLLR FLISDGSHID GDTPYAEVEV
     MKMCMPLLSP ASGIIRFEMS EGQAMQAGEL IARLDLDDPS AVRKAELFHG SFPILGPPTA
     VSGKVHQRCA ASLNAAHMIL AGYEHNIDDV VQNLLACLDS PQLPFLQWQE CFSVLATRLP
     KDLRSELESK FKEFERISSS QIVDFPAKLL KGILEAHITS CPEKEKASQE RLIEPLMSLV
     KSYEGGRESH ARVIVQSLFE EYLSVEELFS DNIRADVIER LRLQYKKDLL KVVDIVLSHQ
     GIKSKNKLIM RLMEQLVYPN PAAYRDKLIR FSVLNHINYS ELALKASQLL EQTKLSELRS
     NIARSLSELE MFTEDGETMD TPKRKSAINE RMEDLVSAPL AVEDALVGLF DHSDHTLQRR
     VVETYVRRLY QPYLVKGSVR MQWHRSGLIA SWEFLEEHIE RKNSAEDETF DKLLVEKHSE
     RRWGAMVIIK SLQFLPAIVH AALRETTHNE AVPNGSSEPK CFGNMMHIAL AGINNQMSLL
     QDSGDEDQAQ ERINKLAKIL KEQELSSSLR TSGVGVISCI IQRDEGRAPM RHSFHWSAEK
     HYYEEEPLLR HLEPPLSIYL ELDKLKGYEN IRYTPSRDRQ WHLYTVKDKP LPIQRMFLRT
     LVRQPTTTGS FTSHQGLDIG SSGSLLASYT SRSILRSLVV AMEELELNAH NATGKYDHAH
     MYLYVVQEQQ VNDLMPYTKR VEVDAKQEEA AVAQILEELA REIHASVGVK MHRLGVSEWE
     VKLWIASSGL ANGAWRFVVT NVTGHTCTTH IYRELEDSST HKVVYHSISV RAPLHGVPVS
     AAYKPLGALE RKRLSARNSN TTYCYDFPLA FQTALEMAWA SHSPNDNNIK NKMLLKVTEL
     KFSDRSGSWG TPLVPVDPEP GSNDFGMVAW CMEMATPEFP SGRTVLVVSN DVTFKAGSFG
     QKEDAFFHAV TDLACAKKLP LIYLAANSGA RLGVAEEVKA RFRVGWSDES NPERGFQYLY
     LTPDDYAEMG SSVIAHELKL ANGETRWVID TIIGKEDGLG VENLTGSGAI AGAYSRAYKE
     TFTLTYVTGR TVGIGAYLSR LGMRCIQRLD QPIILTGFSA LNKLLGREVY SSHMQLGGPK
     IMATNGVVHL TVSDDLEGVS SILKWLSFVP PYVGGPLPIC KPLDPPERPV EYFVENSCDP
     RAAIRGVLDS NGNWVGGIFD KDSFIETLEG WARTVVTGRA KLGGIPVGIV AVETQTVMQI
     IPADPGQLDS HERVVPQAGQ VWFPDSASKT AQAILDFNRE ELPLFILANW RGFSGGQRDL
     FEGILQAGST IVENLRTYKQ PVFVYIPMMG ELRGGAWVVV DSQINPDHIE MYAERTAKGN
     ILEPEGMIEI KFKTKDLIEC MGRLDEELVG LKSKLEESRR AGALEVVNSL QQKIKAREKS
     LLPVYTQMAT KFAELHDTSL RMAVKGVIRE VVDWKTSRSY FYRRLHRRIA EASLIKTVED
     ARGNQLSRTS AYAFMKSWFL NSDVAKGRED AWNDDELFFT WKDDTRNYED KLKELRIQKV
     LQQLTDVGSS ELDLRALPQG LLALLDKMEP SSRASLVQKL LEVLS
//
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