ID E2B9B3_HARSA Unreviewed; 2324 AA.
AC E2B9B3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:EFN87719.1};
GN ORFNames=EAI_14182 {ECO:0000313|EMBL:EFN87719.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN87719.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN87719.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 EMBL; GL446479; EFN87719.1; -; Genomic_DNA.
DR STRING; 610380.E2B9B3; -.
DR EnsemblMetazoa; XM_025305759.1; XP_025161544.1; LOC105192517.
DR InParanoid; E2B9B3; -.
DR OMA; PTPKGHC; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000008237; Unassembled WGS sequence.
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: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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008237}.
FT DOMAIN 101..597
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 254..445
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 724..798
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1546..1886
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1891..2205
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 37..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2116..2145
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2324 AA; 262212 MW; 2A5D38C884F31E12 CRC64;
MKRMKRFVLA EKTVKDPNWK SSDNLLLNVR KIIPKNDEEG GSKYEEKNTD ESGATHPSTL
ESTPSMSQGT VMIQAQSRHQ EKDFTVATPE EFVHRFGGSR VINKVLIANN GIAAVKCMRS
VRRWSYEMFK NERAVRFVVM VTPEDLKANA EYIKMADQYV PVPGGTNNNN YANVELIVDI
AIRTQVQAVW AGWGHASENP KLPELLHKNN ICFIGPSERA MWALGDKIAS SIVAQTADVP
TLPWSGSELK AQYSGKKIKI SSELFRKGCV ASVEECLAAA NKIGFPIMVK ASEGGGGKGI
RKVENAEELP ALFRQVQTEI PGSPIFIMKL AKCARHLEVQ LLADNYGNAI SLFGRDCSIQ
RRHQKIIEEA PAVIAKPEVF EEMEKAAVRL AKMVGYVSAG TVEYLYDTTG RYYFLELNPR
LQVEHPCTEM VSDVNLPAAQ LQIAMGLPLH QIKDIRLLYG ENPWGDNTID FDQPRHKPQP
WGHVIAARIT SENPDEGFKP SSGTVQELNF RSSKNVWGYF SVGASGGLHE FADSQFGHCF
SWGENRDQAR ENLVVALKEL SIRGDFRTTV EYLITLLETE SFLQNNIDTA WLDLLIAERV
RSDKPDLLLA VTCGALHIAD RTITAAFAGF QTALEKGQIQ ASNDLDNVVD VELINDGYKY
KVQAAKSGPN SYFLVMNGSF KEVEVHRMSD GGLLLSLDGA SFTTYMREEV DRYRIVIGNQ
TCIFEKDNDP SLLRSPSAGK LINFLVEDGG HVGASQAYAE IEVMKMVMTV TASEAGSVYY
VKRPGAVLEA GTLIAHLELD DPSLVTKAQE YIGQFPAAAA FAMPEKLNHL HAKYRNALEN
TLAGYCLPDP YHLPRLRELI EKFMFSLRDP NLPLLELQEV IATISGRIPI SVEKKIRKLM
SLYERNITSV LAQFPSQQIA AVIDGHAATL SKRAERDVFF LTTQAIVQLV QRYRNGIRGR
MKTAVHELLR QYYTVESQFQ QGHYDKCVSA LIEKHKDDVA TVTGMIFSHN QVTKKNVLVT
MLIDHLWANE PGLTDELSST LTELTSLNRT EHSRVALRAR QVLIAAHQPA YELRHNQMES
IFLSAVDMYG HDFHPENLQK LILSETSIFD ILHDFFYHCN RAVCNAALEV YVRRAYISYD
LTCLQHLELS GEIPLVYFQF VLPSNHPNRQ NQSLVDHRAG AMAAFQDLEQ FGQYADEVLD
LLEDLSSPTP VVSAKLLEAV DAVGGESRHS TSINVSLSVT ENAATAATSS ATTGDRSADE
PVHILSIAVR EDGTEDDVTM ARLFENWCAS NKDELISRGI RRVTFAALQK KQFPKFFTFR
QRDGFVEDRI YRHLEPGCAF QLELNRMRTY DLEALPTSNQ KMHLYLGQAK VAKGQQVTDY
RFFIRSIIRH SDLITKEASF DYLHNEGERV LLEAMDELEV AFSHPLAKRT ECNHIFLNFV
PTVIMDPARI EESVTSMVLR YGPRLWKLHV RQAEIKMTIR PAPGKPTSNV RLCIANDSGY
SIDLHLYTEA TDPKTGIIRF ESYSPTAANA VNWRPGPMHG LPISTPYMTK DYLQAKRFQA
QSAGTTYVYD LPDMFRQQVE KMWQRYIEER QSSHGSIAMP SPVMDVVELV LDGKQLVEQK
RLPGENDVGM IAWRLTLYTP EYPFGRDIIL IANDLTYMIG SFGTREDLVF CRASERAREL
GCPRIYFSAN SGARIGLAEE VKALFRIAWE DENEPEKGFK YIYLTPDDYT RLAPLNSVKA
SLIEDPTGES RYRITDIIGK DDDLGVENLK YAGLIAGETS RAYEEIITIS VVSCRAIGIG
SYLLRLGQRV IQIENSHIIL TGYRALNAVL GREVYASNNQ LGGTQIMHNN GVSHAIDARD
LDGVATILKW LSYFPKNKGA PLPMLLPVVD SIDREITYMP TKTAYDPRWM LEGRHCSESN
VWESGFFDRG SWHEIMRPWA QTVVTGRARL GGIPCGVIAV ETRTVELHLP ADPANLDSEA
KTISQAGQVW FPDSSYKTAQ AIKDFGKEEI PLFIFANWRG FSGGMKDMYE QIVKFGAYIV
DGLREYCRPV LVYIPPNGEL RGGAWAVVDP TINPRYMEMF ADNTSRAGVL EPEAIVEIKF
RNKDIVKTMH RIDLIIQKLK EKLSAAGTTE ERAELETQIR KREQTLEPMY HQVAVHFAEL
HDTPERMFEK NAIHEIIPWK RARRLFYWRL RRRLLEEEIR TEILSTQPSL DVRQVDAMLR
RWFIEDKGAT ESYLWDQDEA ATCWLEAQRK TENSVVSRNI MCVKRDAVVT RIKEALEACP
EIRLDAVLEI AHRLQPTERA ELQRTLSQLE VTGQEHHTDS SVSS
//
