GenomeNet

Database: UniProt
Entry: A0A0D9ZWV5_9ORYZ
LinkDB: A0A0D9ZWV5_9ORYZ
Original site: A0A0D9ZWV5_9ORYZ 
ID   A0A0D9ZWV5_9ORYZ        Unreviewed;      2436 AA.
AC   A0A0D9ZWV5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM05G10750.2};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM05G10750.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM05G10750.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) 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   -!- 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   STRING; 40148.A0A0D9ZWV5; -.
DR   EnsemblPlants; OGLUM05G10750.2; OGLUM05G10750.2; OGLUM05G10750.
DR   Gramene; OGLUM05G10750.2; OGLUM05G10750.2; OGLUM05G10750.
DR   eggNOG; KOG0368; Eukaryota.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000026961; 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: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; 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:SF4; ACETYL-COA CARBOXYLASE 2; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT   DOMAIN          264..771
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          417..611
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          879..953
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1679..2020
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          2024..2338
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          144..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2436 AA;  269991 MW;  58616D0DFBDE391F CRC64;
     MPMRPWEFII LGRTAPISPP PLGISAFSRA LRLRLAAVVD AARIQTPPRV AFSAFFFFFF
     FFSEGLSREG TAARLPALIY RVPFIPCLLQ LQIRAPHADP RPAGESAADF THLGIYLLFV
     WHYTFEKPTT MTSTHVATLG VGAQAPPRHQ KKSAGTAFVS SGSSRPSYRK NGQRTRSLRE
     ESNGGVSDSK KLNHSIRQGL AGIIDLPNDA ASEVDISHGS EDPRGPTVPG SYQMNGIINE
     THNGRHASVS KVVEFCTALG GKTPIHSVLV ANNGMAAAKF MRSVRTWAND TFGSEKAIQL
     IAMATPEDLR INAEHIRIAD QFVEVPGGTN NNNYANVQLI VEIAERTGVS AVWPGWGHAS
     ENPELPDALT AKGIVFLGPP ASSMHALGDK VGSALIAQAA GVPTLAWSGS HVEVPLECCL
     DSIPDEMYRK ACVTTTEEAV ASCQVVGYPA MIKASWGGGG KGIRKVHNDD EVRTLFKQVQ
     GEVPGSPIFI MRLAAQSRHL EVQLLCDQYG NVAALHSRDC SVQRRHQKII EEGPVTVAPR
     ETVKELEQAA RRLAKAVGYV GAATVEYLYS METGEYYFLE LNPRLQVEHP VTEWIAEVNL
     PAAQVAVGMG IPLWQIPEIR RFYGMNHGGG YDLWRKTAAL ATPFNFDEVD SKWPKGHCVA
     VRITSEDPDD GFKPTGGKVK EISFKSKPNV WAYFSVKSGG GIHEFADSQF GHVFAYGTTR
     SAAITTMALA LKEVQIRGEI HSNVDYTVDL LNASDFRENK IHTGWLDTRI AMRVQAERPP
     WYISVVGGAL YKTVTANTAT VSDYVGYLTK GQIPPKIDTV RSGHGSYRLR MNGSTVDANV
     QTLCDGGLLM QLDGNSHVIY AEEEASGTRL LIDGKTCMLQ NDHDPSKLLA ETPCKLLRFL
     VADGAHVDAD VPYAEVEVMK MCMPLLSPAS GVIHVVMSEG QAMQAGDLIA RLDLDDPSAV
     KRAEPFEDTF PQMGLPIAAS GQVHKLCAAS LNACRMILAG YEHDIDKVVP ELVYCLDTPE
     LPFLQWEELM SVLATRLPRN LKSELEGKYE EYKVKFDSGI INDFPANMLR VIIEENLACG
     SEKEKATNER LVEPLMSLLK SYEGGRESHA HFVVKSLFEE YLYVEELFSD GIQSDVIERL
     RLQHSKDLQK VVDIVLSHQS VRNKTKLILK LMESLVYPNP AAYRDQLIRF SSLNHKAYYK
     LALKASELLE QTKLSDLCAR IARSLSELEM FTEESKVLSM HKREIAIKES MEDLVTAPLP
     VEDALISLFD CSDTTVQQRV IETYIARLYQ PHLVKDSIKM KWIESGVIAL WEFPEGYFDA
     RNGGAVLGDK RWGAMVIVKS LESLSMAIRF ALKETSHYTS SEGNMMHIAL LGADNKMNII
     QESGDDADRI AKLPLILKDN VTDLHASGVK TISFIVQRDE ARMTMRRTFL WSDEKLSYEE
     EPILRHVEPP LSALLELDKL KVKGYNEMKY TPSRDRQWHI YTLRNTENPK MLHRVFFRTL
     VRQPSVSNKF SSGQIGDMEV GSAEEPLSFT STSILRSLMT AIEELELHAI RTGHSHMYLH
     VLKEQKLLDL VPVSGNTVLD VGQDEATAYS LLKEMAMKIH ELVGARMHHL SVCQWEVKLK
     LDCDGPASGT WRIVTTNVTS HTCTVDIYRE MEDKESRKLV YHPATPAAGP LHGVALNNPY
     QPLSVIDLKR CSARNNRTTY CYDFPLAFET AVRKSWSSST SGASKGVENA QCYVKATELV
     FADKHGSWGT PLVQMDRPAG LNDIGMVAWT LKMSTPEFPS GREIIVVAND ITFRAGSFGP
     REDAFFEAVT NLACEKKLPL IYLAANSGAR IGIADEVKSC FRVGWSDDGN PERGFQYIYL
     SEEDYARIGT SVIAHKMQLD SGEIRWVIDS VVGKEDGLGV ENIHGSAAIA SAYSRAYKET
     FTLTFVTGRT VGIGAYLARL GIRCIQRLDQ PIILTGYSAL NKLLGREVYS SHMQLGGPKI
     MATNGVVHLT VSDDLEGVSN ILRWLSYVPA YIGGPLPVTT PLDPPDRPVA YIPENSCDPR
     AAIRGVDDSQ GKWLGGMFDK DSFVETFEGW AKTVVTGRAK LGGIPVGVIA VETQTMMQTI
     PADPGQLDSR EQSVPRAGQV WFPDSATKTA QALLDFNREG LPLFILANWR GFSGGQRDLF
     EGILQAGSTI VENLRTYNQP AFVYIPMAAE LRGGAWVVVD SKINPDRIEC YAERTAKGNV
     LEPQGLIEIK FRSEELQDCM SRLDPTLIDL KAKLEVANKN GSADTKSLQE NIEARTKQLM
     PLYTQIAIRF AELHDTSLRM AAKGVIKKVV DWEESRSFFY KRLRRRISED VLAKEIRAVA
     GEQFSHQPAI ELIKKWYSAS HAAEWDDDDA FVAWMDNPEN YKDYIQDLKA QRVSQSLSSL
     SDSSSDLQAL PQGLSMLLDK MDPSRRAQLV EEIRKA
//
DBGET integrated database retrieval system