ID M8BYH2_AEGTA Unreviewed; 2130 AA.
AC M8BYH2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, 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 Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=37682 {ECO:0000313|EnsemblPlants:EMT11869};
RN [1] {ECO:0000313|EnsemblPlants:EMT11869}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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 EnsemblPlants; EMT11869; EMT11869; F775_16346.
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:SF8; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 2.
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};
KW 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}.
SQ SEQUENCE 2130 AA; 236964 MW; 2B6DB4CC5B0F3A8D CRC64;
MMVKSDQITE FCKALGGDTP IRSVLVANNG MAAVKFMRSI RAWASETFGT DKAVLLVAMA
TPEDLRANAE HVRIADQFLE VPGGTNNNNY ANVQLIVEIA ERTRISAVWP GWGHASEDPE
LPDALKEKGI IFLGPPSAAM AALGDKIGSS LIAQAAGVPT LPWSGSHVKV PQETCHSIPE
EIYKKACVST TEEAVASCQV VGYPAMIKAS WGGGGKGIRK VHNDDEVRAL FKQVQGEVPG
SPIFVMKLAS QSRHLEVQLL CDKHGNVAAL HSRDCSVQRR HQKIIEEGPI TVAPPEKVRE
LEQAARRLAK CVQYQGAATV EYLYSMETGE YYFLELNPRL QVEHPVTEWI AGVNLPASQV
VVGMGIPLYN IPEIRRFYGV EHGGGYHSWK EISAVAAKFD LDKAQSVRPT GHCVAVRVTS
EDPDDGFKPT GGRVEELNFK SKPNVWAYFS VKSGGAIHEF SDSQFGHVFA FGESRSLAIA
NMVLGLKEIQ IRGDIRTNVD YTVDLLNAAE YRENKIHTGW LDSRIAMRVR AERPPWYLSV
VAGALYEASS RSSSVVTDYV GYLSKGQIPP RHISLVNLTV TLNIEGIKYT VKTVRGGPGS
YKLRINESEI EAEMHSLRDG GLLMQLDGNS HKEHDPSKLL ADTPCKLLRF LVADGSHVVA
DTPYAEVEVM KMCMPLLLPA SGVIHFVMPE GQAMQASDLI ARLDLDDPSS VRKAEPFHGT
FPKLGPSAAT SGKVHQKFAA SMNSAHMILA GYEHNISHVV QDLLNCLDSP ELPFLRWQEL
MSVLATRLPK DLRNELDGVY KEYELNADFR NGQDFPAKLI REVIEANLAH CSEKDRITSE
RPIEPLMSLV KSYEGGRESH ACVVVKSLFE EYLSVEELFS DDIQSDVIER LRLQHAKDLE
KVVYIVFSHQ GVKNKNELIL QLMDGLVYPN PSAYRDQLMR FSALNHTAYS GLALKAIEDA
LVALFDHSDP TLQRRVVETY IRRLYEHYLV RGSVRIQWHR SGLIALWEFS EEHIGQSATL
LKQHVKDPRG RRWGVMVVIK SLQCLSTAIE AALKETSHYR AGAGSVSDGN PINSNHGNIL
HIALVGISNQ MSTLQDSGDE DQAQERINKL SKILKETITS HLNGAGVRVV SCIIQRDEGR
PPMRHSFKWS FDKLYYEEDP MLRHVEPPLS TFLELDKVHL EGYSDAKYTP SRDRQWHIYT
LVNNSRDPRS NDQRMFLRTI VRQPSVTNGF SFGNIDNEVC RAQASSSLIS NSILRSLMAA
LEEVELHAHN EAVRSGHSHM YMCILREQRL FDLIPVSRRT DEVGQDEETA CTLLKHMATN
IHEHVGVRMH RLSVCQWEVK LWLDCDGQAS AGPLHGIPLH EPYKPLDALD QKLNTARKNE
TTYCYDFPLV FEKALKESWK SGISHVAEAN GHNQRYAQVT ELMFADSTGS WGTPLVPVER
PPGMNDIGTV AWKMKLSTPE FPDGREIIVV ANDVTFKAGS FGPREDAFFD AVTNLACERK
IPLIYLAATS GARLGVADEI KACFHVGWSD DEIPERGFHY IYLMDQDYSR LRSSVIAHEL
KLESGETRWV VDTIVGKEDG LGCENLHGSG AIASAYSKAY RETFTLTFVT GKAVGIGAYL
ARIGMRCIQR LDQPIILTGF SPLNKLLGRE VYSSQLQLGG PKIMAANGVA HLTVSDDLEG
VSAILKWLSY VPPYVGGPLP ILKPLDPPER PVTYFPQNSC DARAAICGLQ EDTQGGKWLG
GMFDRESFVE TLGGWAKTVI TGRAKLGGIP VGVIAVETET MMQVTPADPG QLDSAERVVP
QAGQVWFPDS AAKTAQALLD FNHEELPLFI LANWRGFSGG QRDLFEGILQ AGSMIVENLR
TYKQPAFVYI PKAGELRGGA WVVVDSKVNP EHIEMYAERS AKGNVLEPKA LIEIKFKPNE
VEESMLRLDP QLARLNARLL QEIKTGTSET ESIRIRSMMA ARTKQLMPIY TQVATWFAEL
HDTTSRMIAK GVISKVVDWE ESRAFFFRRL RRRVAEDSLA KQVREAAGEQ MMPTHGLALE
RIKEWHMASQ GQGDGDNWND DEAFFAWKDD CSNYDKYLEE LKAARVSRLL SQLAESSDVK
ALPNGLSLLL GQMNPSKREQ VIDGLRQLLG
//
