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Database: UniProt
Entry: A0A0E0KZL1_ORYPU
LinkDB: A0A0E0KZL1_ORYPU
Original site: A0A0E0KZL1_ORYPU 
ID   A0A0E0KZL1_ORYPU        Unreviewed;      2445 AA.
AC   A0A0E0KZL1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC05G06090.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC05G06090.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC05G06090.1}
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}.
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DR   STRING; 4537.A0A0E0KZL1; -.
DR   EnsemblPlants; OPUNC05G06090.1; OPUNC05G06090.1; OPUNC05G06090.
DR   Gramene; OPUNC05G06090.1; OPUNC05G06090.1; OPUNC05G06090.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_2_1; -.
DR   OMA; EEPILRH; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000026962; Chromosome 5.
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:UP000026962}.
FT   DOMAIN          252..759
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          405..599
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          886..960
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1686..2027
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          2031..2345
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          96..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2445 AA;  270231 MW;  38FCB9A83500B8DB CRC64;
     MRPWEFIILG RTAPIPPPPL GISAFSRPLR LRLAAAAAAV VDAARIQTPP RVAFSASCFF
     FFFFFFFSEG ISREGTPARL PALIYRLRFI RRAPSVHSVP SPAPDPRAAR RSAPGRTTMT
     STHVATLGVG AQAPPRHQKK SAGTAFVSSG SSRSSYRKNG QRTRSLREES NGGVSDSKKL
     NHSIRQGLAG IIDLPNDAAS EVDISHGSED PRGPTVPGSY QMNGIINETH NGRHASVSKV
     VEFCTALGGK TPIHSVLVAN NGMAAAKFMR SVRTWANDTF GSEKAIQLIA MATPEDLRIN
     AEHIRIADQF VEVPGGTNNN NYANVQLIVE IAERTGVSAV WPGWGHASEN PELPDALTAK
     GIVFLGPPAS SMHALGDKVG SALIAQAAGV PTLAWSGSHV EVPLECCLDS IPDEMYRKAC
     VTTTEEAVAS CQVVGYPAMI KASWGGGGKG IRKVHNDDEV RTLFKQVQGE VPGSPIFIMR
     LAAQSRHLEV QLLCDQFGNV AALHSRDCSV QRRHQKIIEE GPVTVAPRET VKELEQAARR
     LAKAVGYVGA ATVEYLYSME TGEYYFLELN PRLQVEHPVT EWIAEVNLPA AQVAVGMGIP
     LWQIPEIRRF YGMNHGGGYD LWRKTSALAT PFNFDEVDSK WPKGHCVAVR ITSEDPDDGF
     KPTGGKVKEI SFKSKPNVWA YFSVKSGGGI HEFADSQFGH VFAYGTTRSA AITTMALALK
     EVQIRGEIHS NVDYTVDLLN ASDFRENKIH TGWLDTRIAM RVQAERPPWY ISVVGGALYK
     TVTANTATVS DYVGYLTKGQ IPPKHISLVY TTVALNIDGK KYTIETVRSG HGSYRLRMNG
     SMVEANVQTL CDGGLLMQLD GNSHVIYAEE EASGTRLLID GKTCMLQNDH DPSKLLAETP
     CKLLRFLVAD GAHVDADVPY AEVEVMKMCM PLLSPASGVI HVVMSEGQAM QAGDLIARLD
     LDDPSAVKRA EPFDDTFPQM GLPIAASGQV HKLCASSLNA CRMILAGYEH DIDKVVPELV
     YCLDTPELPF LQWEELMSVL ATRLPRNLKS ELEGKYEECK VKFDSGIIND FPAKMLGVTI
     EENLACGSEK EKATNERLVE PLMSLLKSYE GGRESHAHFV VKSLFEEYLY VEELFSDGIQ
     SDVIERLRLQ HSKDLQKVVD IVLSHQSVRN KTKLILKLME SLVYPNPAAY RDQLIRFSSL
     NHKAYYKLAL KASELLEQTK LSELRARIAR SLSELEMFTE ESKGLSMHQR EIAIKESMED
     LVTAPLPVED ALISLFDCSD TTVQQRVIET YIARLYQPHL VKDSIKMKWI ESGVIALWEC
     PEGHFDARNG GAVLGDKRWG AMVIVKSLES LSMAIRFALK ETSHYTSSEG NMMHIALFGA
     DNKMNIIQES GDDADRIAKL PLILKDNVTD LHASGVKTIS FIVQRDEARM TMRRTFLWSD
     DKLSYEEEPI LRHVEPPLSA LLELDKLKVK GYNEMKYTPS RDRQWHIYTL RNTENPKMLH
     RVFFRTLVRQ PSVSNKFSSG QIGDMEVGSA EEPLSFTSTS ILRSLMTAIE ELELHAIRTG
     HSHMYLHVLK EQKLLDLVPV SGNIVLDVGQ DEATAYSLLK EMAMKIHELV GARMHHLSVC
     QWEVKLKLDC DGPAGGTWRI VTTNVTSHTC TVDIYREVED TEARKLVYHS ASPAAGPLHG
     VALNNPYQPL SVIDLKRCSA RNNRTTYCYD FPLAFETAVR KSWSSSTSGA SKGVENAQCY
     VKATELVFAD KHGSWGTPLA QMDRPAGLND IGMVAWTLKM STPEFPSGRE IIVVANDITF
     RAGSFGPRED AFFEAVTNLA CEKKLPLIYL AANSGARIGI ADEVKSCFRV GWSDDGSPER
     GFQYIYLSEE DYARIGTSVI AHKMQLDSGE IRWVIDSVVG KEDGLGVENI HGSAAIASAY
     SRAYKETFTL TFVTGRTVGI GAYLARLGIR CIQRLDQPII LTGYSALNKL LGREVYSSHM
     QLGGPKIMAT NGVVHLTVSD DLEGVSNILR WLSYVPAYIG GPLPVTTPLD PPDRPVAYIP
     ENSCDPRAAI RGVDDSQGKW LGGMFDKDSF VETFEGWAKT VVTGRAKLGG IPVGVIAVET
     QTMMQTIPAD PGQLDSREQS VPRAGQVWFP DSATKTAQAL LDFNREGLPL FILANWRGFS
     GGQRDLFEGI LQAGSTIVEN LRTYNQPAFV YIPMAAELRG GAWVVVDSKI NPDRIECYAE
     RTAKGNVLEP QGLIEIKFRS EELQDCMGRL DPTLIDLKAK LEAANKNGSA DTKSLQENIE
     ARTKQLMPLY TQIAIRFAEL HDTSLRMAAK GVIKKVVDWG ESRSFFYKRL RRRISEDVLA
     KEIRAVAGEQ FSHQPAIELI KKWYSASHAA EWDDDDAFVA WMDNPENYKD YIQDLKAQRV
     SQSLSSLSDS SSDLQALPQG LSMLLDKMDP SRRAQLVEEI RKVLG
//
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