ID E5LBD5_ECHCG Unreviewed; 2316 AA.
AC E5LBD5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
OS Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Boivinellinae; Echinochloa.
OX NCBI_TaxID=90397 {ECO:0000313|EMBL:ADR32359.1};
RN [1] {ECO:0000313|EMBL:ADR32359.1}
RP NUCLEOTIDE SEQUENCE.
RA Huan Z., Jin T., Bi Y., Wang J.;
RT "Resistance to quizalofop endowed by ACCase point mutation in barnyard
RT grass (Echinochloa crus-galli).";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR32359.1}
RP NUCLEOTIDE SEQUENCE.
RA Huan Z.-B., Jin T., Zhang S.-Y., Wang J.-X.;
RT "Cloning and sequence analysis of plastid acetyl-CoA carboxylase cDNA from
RT two Echinochloa crus-galli biotypes.";
RL J. Pestic. Sci. 36:461-466(2011).
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 EMBL; HQ395759; ADR32359.1; -; mRNA.
DR SMR; E5LBD5; -.
DR UniPathway; UPA00655; UER00711.
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 2: Evidence at transcript level;
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 131..638
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 284..478
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 765..839
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1556..1892
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1896..2212
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2316 AA; 255591 MW; F30960E40DA59500 CRC64;
MSQLGLAAAA SKALPLLPNR QRSSAGPTFP SSPSVRPSNR RKSRTRSLRD GGDGVSDAKK
HNQSVRQGLA GIIDLPNEAT SEVDISHGPE DPRWPAESCQ MNGIINEIHN GRHASVSNVV
EFCAALGGKT PIHSILVANN GMAAAKFMRS VRTWANDTLG SERAIQLIAM ATPEDMRINA
EHIRIADQFV EVPGGTNNNN YANVQLIVEV AERVGVSAVW PGWGHASENP ELPDALTAKG
IVFLGPPASS MNALGDKVGS ALIAQAAGVP TLSWSGSHVE VPLECCLDAI PEEMYRKACV
TTTEEAVASC QVVGYPAMIK ASWGGGGKGI RKVHNDDEVR ALFKQVQGEV PGSPIFIMRL
ASQSRHLEVQ LLCDQYGNVA ALHSRDCSVQ RRHQKIIEEG PVTVAPRETV KALEQAARRL
AKAVGYVGAA TVEYLYSMET GEYYFLELNP RLQVEHPVTE WIAEVNLPAA QVAVGMGIPL
WQIPEIRRFY GMDYGGGYDI WRKTAALATP FNFDEVDSQW PKGHCVAVRI TSEDPDDGFK
PTGGKVKEIS FKSKPNVWAY FSVKSGGGIH EFADSQFGHV FAYGLSRSAA ITNMTLALKE
IQIRGEIHSN VDYTVDLLNA SDFRENKIHT GWLDTRIAMR VQAERPPWFI SVVGGALYKT
VTANAATVSD YVSYLTKGQI PPKHISLVNS TVNLNIEGSK YTIETARTGY GSYRLRLNGS
AIEANVQSLC DGGLLMQLDG NSHVIYAEEE AGGTRLLIDG KTCLLQNDHD PSKLLAETPC
KLLRFLVADG AHVDADVPYA EVEVMKMCMP LLSPASGVIH VMMSEGQALQ AGDLIARLDL
DDPSAVKRAE PFHGMFPQMG LPVAASSQVH KRYAASLNAA RMVLAGYEHN INEVVQDLVC
CLDDPELPFL QWDELMSVLA TRLPRNLKSE LEDKYKEYKL NFYHGKNKDF PSKLLSNIIE
ANLAYGSEKE KATNKRLVEP LMSLLKSYEG GRESHAHFVV KSLFEDYLAV EELFSDGIQS
DVIETLRHQH SKDLQKVVDV VLSHQGVRSK AKLVIALMEK LVYPNPAAYR DLLVRFSSLN
HKRYYKLALK ASELLEQTKL SELRASIARS LSDLGMHKGE ITINDSMEDL VSTPLPVEDA
LISLFDYSDP TVQQKVIVTY ISRLYQPLLV KDSIQLKFKE PGAFASWEFS EGHVDAENGQ
GAVSARKRCG AMVVLKSLES ARTAIVAALK DLSQHASSEG NMMHIALLSA ENENNFSDDQ
AQHRMENLTK ILKDTSVVND LRAAGLKVIC CIVQRDEARM PMRHTFLWSD EKSCYEEEQI
LRHVEPPLSA LLELDKLKVK GYNEMKYTPS RDRQWHIYTL RNTENPKMLH RVLFRTIVRQ
PNAGNKFTSA LIGNPEIGGP EESLSFTSNS ILRSLMTAIE ELELHAIRTG HSHMYLCILK
EQKLLDLIPF SGSTIVDVGQ DEATACSLLK SMALKIHELV GAQMHHLSVC QWEVKLKLDC
DGPASGTWRV VTTNVTSHTC TVDIYREVED TELQKLVYHS ASSSASPLHG VALNNPYQPL
SVIDLKRCSA RNNRTTYCYD FPLVFETALQ KSWQSNGSSG SSKTYVKATE LVFAEKHGSW
GTPIIPMERP AGLNDIGMVA WILEMSTPEF PNGRQIIVVA NDITFRAGSF GPREDAFFEA
VTNLACERKL PLIYLAANSG ARIGIADEVK SCFRVGWSDE GSPERGFQYI YLTEEDYDRI
SSSVIAHKLQ LDSGEVRWII DSVVGKEDGL GVENLHGSAA IASAYSRAYE ETFTLTFVTG
RTVGIGAYLA RLGIRCIQRL DQPIILTGFS ALNKLLGREV YSSHMQLGGP KIMATNGVVH
LTVSDDLEGV SNILRWLSYV PANIGGHLPI TKPLDPPDRP VAYIPENTCD PRAAIRGVDD
SQGKWLGGMF DKDSFVETFE GWAKTVVTGR AKLGGIPVGV IAVETQTMMQ LIPADPGQLD
SHERSVPRAG QVWFPDSATK TAQALLDFNR EGLPLFILAN WRGFSGGQRD LFEGILQAGS
TIVENLRTYN QPAFVYIPMA GELRGGAWVV VDSKINPDRI ECYAERTAKG NVLEPQGLIE
IKFRSEELQD CMGRLDPELI NLKAKLQGAK VGNGSIPDIE SLQKSIEART KQLLPLYTQI
AIRFAELHDT SLRMAAKGVI KKVVDWEESR SFFYKRLRRR ISEDVLAKEI RGIAGDHFTH
QSAVELIKEW YLASLAATGN TEWDDDDAFV AWKDNPENYK GYIQELRAQK VSQSLSDLAG
SSSDLEAFSQ GLSTLLDKMD PSQRAKFAQE IKKVLG
//
