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Database: UniProt
Entry: A0A1U7V9F9_NICSY
LinkDB: A0A1U7V9F9_NICSY
Original site: A0A1U7V9F9_NICSY 
ID   A0A1U7V9F9_NICSY        Unreviewed;      2266 AA.
AC   A0A1U7V9F9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Acetyl-CoA carboxylase 1-like {ECO:0000313|RefSeq:XP_009758450.1};
GN   Name=LOC104211137 {ECO:0000313|RefSeq:XP_009758450.1};
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009758450.1};
RN   [1] {ECO:0000313|Proteomes:UP000189701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA   Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA   Peitsch M.C., Ivanov N.V.;
RT   "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT   tomentosiformis.";
RL   Genome Biol. 14:R60.1-R60.17(2013).
RN   [2] {ECO:0000313|RefSeq:XP_009758450.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_009758450.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_009758450.1; XM_009760148.1.
DR   STRING; 4096.A0A1U7V9F9; -.
DR   GeneID; 104211137; -.
DR   KEGG; nsy:104211137; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000189701; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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: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; 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   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
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}; Plastid {ECO:0000256|ARBA:ARBA00022528};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189701}.
FT   DOMAIN          47..554
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          200..392
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          1505..1844
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1848..2163
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   2266 AA;  252624 MW;  941029BB50334F4C CRC64;
     MSEAQRMPTM IRIKSGNGHV NGALPLRSPM ARAEVAEFCN ALGGKRPINS ILIANNGMAA
     VKFIRSIRTW AYETFGTEKA ILLVAMATSE DMRINAEHIR IADQFVEVPG GTNNNNYANV
     QLIVEMAEMT HVDAVWPGWG HASENPELPD ALNAKGIIFL GPPATSMAAL GDKIGSSLIA
     QAAEVPTLPW SGSNVKVPPE SSLVSIPDEI YAKACVHTTE EAIASCQDVG FPAMIKASWG
     GGGKGIRKVH NDDEVRALFK QVQGEVPGSP IFIMKVASQS RHLEVQLLCD QYGNVAALHS
     RDCSVQRRHQ KIIEEGPITV APQDTVKKLE QAARRLAISV NYVGAATVEY LYSMDTGEYY
     FLELNPRLQV EHPVTEWIAE INLPAAQVAV GMGIPLWQIP EIRRFYGMEH GAGYDAWRKT
     SIAATPFDFD KAESTRPKGH CVAVRVTSED PDDGFKPTSG KVQELSFKSK PNVWAYFSVK
     SGGGIHEFSD SQFGHVFAFG ESRALAIANM VLGLKEIQIR GEIRTNVDYT IDLLHASDYR
     ENKIHTGWLD SRIAMRVRAE RPPWYLSVVG GALYKASASG AALVSEYIGY LEKGQIPPKH
     ISLVSSQVSL NIEGSKYTIN MVRGGPGSYR LRMNESEIEA EIHTLRDGGL LMQLDGNSHV
     IYAEEEAAGT RLLIDGRTCL LQNDHDPSKL IAETPCKLLR YLMSDGSHVD ADTPYAEVEV
     MKMCMPLLSP ASGVIHFKMS EGQAMQAGEL IASLDLDDPS AVRKAEPFRG SFPILEPPTA
     ISGKVHQRCA ASLNATRMIL AGYDHNVDDV VHNLLSCLDS PELPFLQWQE CLSVLATRLP
     KDLRYELEAK YKEYEGISGL QTVDFPARIL RGVLEAHLRT CSEKEKGAQE RLVEPLMSLV
     KSYEGGRESH ARGIVHSLFE EYLTVEELFS DNIQADVIER LRLQYKKDLL KVVDIVLSHQ
     GVRRKNKLIL SLMEQLVYPN PAAYREKLIR FSALNHTNYS ELALKASQLL EQTKLSELRS
     SIARNLSELE MFTEEGDSMD TPKRKSAINE RMEVLVSAPL AVEDALVGLF DHSDHTLQRR
     VVETYIRRLY QPYLVQGSVR MQWHRSGLIA TWQFMEEHVE RKSGSGGDNV IVKPLVEKHS
     ERKWGAMVII KSLQLLPTVL NSALRETAHD LHAEMSNGST QPVSHGNMLH IALVGINNQM
     SLLQDSGDED QAQERIYKLA KILRDKDASA SLKSAGVGVI SCIIQRDEGR VPMRHSFHWS
     TEKLYYEEEA LLRHLEPPLS IYLELEKLKI YDNIKYTPSR DRQWHLYTVV DKQNPIQRMF
     LRTLVRQPTD DGLLAYQGLN QGTAHSSLNL PFTSRSILRS LISALEELEL NLHNSTLKAD
     HAHMYLYILR EQEFDDLLPY HKRADVNNEH KEAEVQKILE ELAHEINASV GVRMHRLGVC
     EWEVKLWISS AGDATGAWRI VVANVTGHTC IVHIYREVED TGVQRVVYHS AIGHGPLNGV
     PVTAPYPPLA VLDQKRLLAR KNDTTYCYDF PLAFKAALEK SWASHNPGTD KPKDNVLLKV
     TELTFVDKKG SWGTPLVPVE RQPGFNDVGM VAWIMEMSTP EFPTGRKILV VANDVTFING
     SFGPSEDAFF QAVTGVSCTQ KLPLIYLAAN SGARIGAAEE VKSCFKVGWS DESNPERGFQ
     YIYLIPEDHE RIKSSVMAHE LKLSNGEVRW VIDTIIGEED GLGVENLSGS GAIASAYSRA
     YHETFTLTYV TGRTVGIGAY LARLGMRCIQ RLDQPIILTG YSALNKLLGR EVYSSHMQLG
     GPKIMGTNGV VHLTVSDDLE GISKILNWLS FVPPYSGGPL PISTPLDPPQ RPVEYFPETA
     CDPRAAISGH TDASGKWLGG IFDKDSFIET LEGWARTVVT GRAKLGGIPV GIVAVETQTM
     MQVIPADPGQ LDSHERVVPQ AGQVWFPDSA TKTAQALMDF NREELPLFIL ANWRGFSGGQ
     RDLFEGILQA GSTIVENLRT YKQPVFVYIP MMGELRGGAW VVVDSKINSD HIEMYAERTA
     KGNVLEPEGM IEIKFRTKEL LECMGRLDQQ LINLKLKLQE ARTAGVYTNV EALQQQIKTR
     ETQLLPVYTQ IATKFAELHD TSLRMAAKGV IREVVNWETS RSFFYRRLLR RVEEEMLVKT
     VRNAAGDQLS YKSAMDMVKT WFLDSKGGKV DSWIDDEAFF SWKNDPKNYE EQLQQLRVQK
     VLVQLSKIGD STLDLRALPQ GLLSLLQKVE PATREQLISD LKKLLN
//
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