ID A0A1W4XI45_AGRPL Unreviewed; 2227 AA.
AC A0A1W4XI45;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acetyl-CoA carboxylase isoform X5 {ECO:0000313|RefSeq:XP_018332457.1};
GN Name=LOC108741969 {ECO:0000313|RefSeq:XP_018332457.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018332457.1};
RN [1] {ECO:0000313|RefSeq:XP_018332457.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018332457.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001455};
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 RefSeq; XP_018332457.1; XM_018476955.2.
DR SMR; A0A1W4XI45; -.
DR EnsemblMetazoa; XM_018476955.2; XP_018332457.1; LOC108741969.
DR GeneID; 108741969; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000192223; Unplaced.
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; IPR001882; Biotin_BS.
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:SF3; ACETYL-COA CARBOXYLASE; 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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00866; CPSASE_1; 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:UP000192223}.
FT DOMAIN 1..480
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 607..681
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1437..1776
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1780..2113
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2227 AA; 252014 MW; 3C4557AEF5A7E4C2 CRC64;
MRSVRRWSYE MFKNERAVRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGTN NHNYANVELI
VDIAIRCQVQ AVWAGWGHAS ENPKLPELLH KNDIAFIGPP EKAMWALGDK IASSIVAQTA
DIPTLPWSGS DLKAQYTGKR IKISSDLFSK GCVHSAEQGL AACQKIGFPV MIKASEGGGG
KGIRKVESAD DFPSAFRQVQ AEVPGSPIFV MKLAKCARHL EVQLLADQYG NAISLFGRDC
SIQRRHQKII EEAPAVIAKP EIFEEMEKAA VRLAKMVGYI SAGTVEYLYD VSGKYYFLEL
NPRLQVEHPC TEMVSDVNLP AAQLQIAMGL PLHYIKDIRM LYGESPWGTF EIDFDAPLHK
PEPWGHVIAA RITSENPDEG FKPSSGTVQE LNFRSSKNVW GYFSVAASGG LHEFADSQFG
HCFSWGENRE QARENLVIAL KELSIRGDFR TTVEYLITLL ETKDFQENTI DTAWLDILIS
EHVQAEKPDV MLAVMCGSLH IAEKTINNAF TEFQNSLEKG QIQGSNALTN VVDVELIHEG
NKYKVQTTKS GPNTYFLVLN GSFKEIEVHR LSDGGILLSV DGASFTTYMK EEVDRYRIVI
GNQTCVFEKE NDPTILRSPS AGKLIGYLVE DGGHVDKGQT YAEIEVMKMV MTLTATESGS
IFFCKRPGAV LDAGSVIATL ELDDPSLVTK AQLYKGPFPE LDVSTPVHSN KLNHIHNTYK
SALESILAGY CLPDPYNVPR LREIIEKFMS SLRDPSLPLL ELQEVMASIS GRIPAAVEKK
IRRLMSLYER NITSVLAQFP SQQIASVIDS HAASMQKRAE RDGFFLATEG IVHLVQRYRN
GIRGRMKAAI QDLLKQYYEV ESQFQQGSYD KCVATLREKN KDDMAVVLAT IFSHSQVAKK
NLLVAMFLDH LWSKEPGLTE ELATTLNELT SLNKSEHSRV ALRARQILIA AHQPAYELRH
NQMESIFLSA VDMYGHEFHP ENLQKLIASE TAIFDILHDF FYHANRAVCH AALEVYVRRA
YTSYDLNCLQ HLELSTETPV VHFQFVLPPS HPNRLSRLDT LRDQLKSQEE EGTDLTKLAH
DTFQRTGCII AFNTIQEFEE ATDEILDLLE DCASPAAISA KDLSMLESGS ESRGNSTSIN
VSISVAESGR QKDEEEITEP NHILQVCIKD KGDTNDSSMS RMFGSYCAKH REELESRGIR
RITFAVLKNK QYPKYFTYRH RDGYKEDRIY RHLEPASAYE LELDRMRTYN LEALPTSNQK
MHLYLGKAKV APGQEVTDYR FFIRSIIRHP DLITKEASFE YLQNEGERAL LEAMDELEVA
FSHPQSRRTD CNHIFLNFMP TVIMDPTKIE EAVTNMVMRY GPRLWKLRVL QAELKMPIRI
NPNAPLQSLR LTLANDSGYY LDINMYTEIL DPEAGIMRFQ AYGTKQGPMH GLPTTTPYLA
KDYLQQKRFQ AQSSGTTYVY DYIDMFRQMI DSHWKLYSEK RNEAVKTPDK QLDFVELVLD
PETETRLVET KRIPGENNVG MVAWRLTLYT PEYPDGRDII VIANDITYQI GSFGPREDKV
FGLASEVARQ LRIPRVYIAA NSGARIGLAE EVKKLFRVAW DDPNEPDKGF KYLYLTPEDY
AKLSTLNSVR AVLIEDEGES RYKITDIIGK EDGLGVENLR YAGMIAGETS QAYNEVVTIS
MVSCRAIGIG SYLVRLGQRV IQIENSHIIL TGYMALNKLL GREVYASNNQ LGGIQIMYNN
GVTHKTEPTD IEGINTILKW LSFIPKDKMS PLPIINSLDP IDREVEYTPT KTPYDPRWML
AGRENLSNPG EWESGFFDRD SFSEIMAPWA QTVVTGRARL GGIPVGVIAV ETRTVELKLP
ADPANLDSEA KTVSQAGQVW FPDSAYKTAQ AIQDFSREDL PLIIFANWRG FSGGMKDMYE
QVMKFGAYIV DGLRQYNQPI IIYIPPNGEL RGGAWAVVDP TINSRHMEMY ADPDSRGGVL
EPEGIVEIKF RKKDLLKAIH RLDPEIVELN KKINEINKLQ PVERKSSITQ QVERPKNPEV
LELEKKVAER EKILLPMYHQ VSVHFADLHD TPERMHEKGV INEVVPWRNS RKILYWRLRR
RLLQNRVISS MTEIQPTIAV GQAESMLRRW FVEDKGPIES YKWENNESVV LWLEDQLSRP
AEQSIIGYNL HCVSKDAALT KIQESLESCP DVALDAVVQI VQKLKDNQKA EVIRTLSLLQ
DDQESPE
//
