ID T1SHX4_9POAL Unreviewed; 2090 AA.
AC T1SHX4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
DE Flags: Fragment;
OS Beckmannia syzigachne.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Poodinae;
OC Beckmanniinae; Beckmannia.
OX NCBI_TaxID=368345 {ECO:0000313|EMBL:AGT45921.1};
RN [1] {ECO:0000313|EMBL:AGT45921.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JYJD-R {ECO:0000313|EMBL:AGT45921.1};
RA Pan L., Dong L., Li J.;
RT "Cross-resistance patterns to ACCase-inhibiting herbicides conferred by
RT mutant ACCase isoforms in American sloughgrass (Beckmannia
RT syzigachneSteud.).";
RL Submitted (AUG-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 -!- 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; KF501582; AGT45921.1; -; Genomic_DNA.
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 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, ECO:0000313|EMBL:AGT45921.1};
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 1..429
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 75..269
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 556..630
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1351..1686
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1690..2003
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGT45921.1"
FT NON_TER 2090
FT /evidence="ECO:0000313|EMBL:AGT45921.1"
SQ SEQUENCE 2090 AA; 232752 MW; D7281F832BD62B61 CRC64;
IAERTGVSAD WPGWGHASEN PELPDALTAK GIVFLGLPAS LMNALGDKVG SALIAQAAGV
RTLAWSGSHV EIPLELCLDS IPEEMYRKVC VTTADEAVAS CEMIGYLAMI KASWRDEGKG
IRKVTNNDEV KALYKQVQCE VPGSLIYIMR LASQSRHLEV QLLCDEYRNV AALHSCDCSV
ERRQQKIIEE WPVTVAPRET MKELEQAARR LAKAVGYVGA ATVEYLYSME TGEYYFLELN
PRLQVEHPVT EWIAEVNLPA AQVAVGMGIP LWQVPEIRRF YGMDNGGGYD IWRKTAALAT
PFNFDEVDSQ WPKGHCVAVR ITSENPDDGF KPTGGKVKEI SFKSKPNVWG YFSVKSGGGI
HEFADSQFGH VFAYGVTRSA AITNMSLALK EIQIRGEIHT NVDYTVDLLN APDFRENTIH
TGWLDTRIAM RVQAERPPWY ISVVGGALYK TITTNAETVS EYVSYLIKGQ IPPKHISLVH
STISLNIEES KYTIEIVRSG QGSYRLRMNG SLVEANVQTL CDGGLLMQLD GNSHVIYAEE
EAGGTRLLID GKTCLLQNDH DPSRLLAETP CKLLRFLIAD GAHVDADVPY AEVEVMKMCM
PLLSPAAGVI NVLLSEGQAM QAGDLIARLD LDDPSAVKRA EPFEGSFPEM SLPIAASGQV
HKRCAASLNA ARMVLAGYDH AVNKVVQDLV WCLDTPELPF LQWEELMSVL ATRLPRRLKS
ELEGKYNEYK LNVDHVKIKD FPTEMLRETI EENLAYVSEK EMVTIERLVD PLMSLLKSYE
GGRENHAHFI VKSLFEEYLS VEELFSDGIQ SDVIERLRLQ YSKDLQKVVD IVLSHQGVRN
KTKLILTLME KLVYPNPAAY RDQLIRFSSL NHKRYYKLAL KASELLEQTK LSELRTSIAR
NLSALDMFTE ERADFSLQDR KMAINESMED LVTAPLPVED ALVSLFDCSD QTLQQRVIET
YISRLYQPQL VKGSIQLKYQ DSGVIALWEF TEENPEKRLG AMVILKSLES VSTAIGAALK
DASHYASSAG NTLHIALLDA DTQMSTTEDS GDNDLAQDRM DKLSLILKQD IVMADLRAAG
VKVISGIVQR HGALMPMRRT FLLSEEKLCY EEEPILRHVE PPLSALLELD KLKVKGYNEM
KYTPSRDRQW HIYTLRNTEN PKMLHRVFFR TVVRQPSAGN RFTSDHISDV EVGHAEESLS
FTSSSILRSL MIAKEELELH AIRTGHSHMY LCILKEQKLL DLVPVSGSTV VDVGQDEATA
CSLLKEMALK IHELVGARMH HLSVCQWEVK LKLDSDGPAS GSWRVVTTNV TGHTCTVDIY
REVEDTESQK LVYHSAAPSS GPLHGITLNN SYQPLSVIDL KRCSARNNRT TYCYDFPLAF
ETAVRKSWSN ISSENNQCYV KATELVFAEK NGSWGTPIIP MQRAAGLNDI GMVAWILDMS
TPEFPSGRQI IVIANDITFR AGSFGPREDA FFEAVTNLAC EKKLPLIYLA ANSGARIGIA
DEVKSCFRVG WADDSSPERG FRYIYLSDED HDRISSSVIA HKMQLDSGEI RWVIDSVVGK
EDGLGVENIH GSAAIASAYS RAYEETFTLT FVTGRTVGIG AYLARLGIRC IQRTDQPIIL
TGFSALNKLL GREVYSSHMQ LGGPKIMATN GVVHLTVPDD LEGVSNILRW LSYVPANIGG
PLPITKSLDP IDRPVAYIPE NTCDPRAAIS GIDDSQGKWL GGMFDKDSFV ETFEGWAKTV
VTGRAKLGGI PVGVIAVETQ TMMQLVPADP GQPDSHERSV PRAGQVWFPD SATKTAQAML
DFNREGLPLF ILANWRGFSG GQRDLFEGIL QAGSTIVENL RTYNQPAFVY IPKAAELRGG
AWVVIDSKIN PDRIECYAER TAKANVLEPQ GLIEIKFRSE ELQECMGRLD PELIDLKTRL
QGANGSLSDG ESLQKSIEAR KKHLLPLYTQ IAVRFAELHD TSLRMAAKGV IRKVVDWEDS
RSFFYKRLRR RISEDVLAKE IRVVIGEKFS HQSAIELIKK WYLASEAAVA GSTGWDDDDA
FVAWRENPEN YNEYIKELRA QRVSQLLSDV ADSSSDLQAL PQGLSMLLDK
//
