ID M7BIG2_CHEMY Unreviewed; 2156 AA.
AC M7BIG2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:EMP37706.1};
GN ORFNames=UY3_04987 {ECO:0000313|EMBL:EMP37706.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP37706.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB521250; EMP37706.1; -; Genomic_DNA.
DR STRING; 8469.M7BIG2; -.
DR eggNOG; KOG0368; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
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:InterPro.
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; 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 PANTHER; PTHR45728:SF5; ACETYL-COA CARBOXYLASE 1; 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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 117..618
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 275..466
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1531..1898
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1902..2040
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2156 AA; 242433 MW; A8D86553B77ABC51 CRC64;
MEESSPTTKP LELNLNSHFI LGSVSEDNSE DETSSLVKLD LLEEKERSLS PVSVCSDSLS
DPGLSNVQDV LASHIRPSMS GLHLVKQGRD RKKVDLQRDF TVASPAEFVT RFGGNKVIEK
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
GANNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLHKNGIAFM GPPSQAMWAL
GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFQKRILS VPQELYEKGY VKDVDDGLLA
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATSVV FEHMEQCAVK LAKMVGYVSA
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL HRIKDIRVMY
GVSPWGDVPI DFENSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
ESFQQNSIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSFRNSVSN FLHSLERGQV
LPAHTLLNTV DVELIYDGRK YVLKVTRQSP NSYVVVMNNS YVEVEVHRLS DGGLLLSYDG
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSLLRSPSAG KLIQYVVEDG GHVFSGQCFA
EIEADLHTGT LPQIHSTALR GEKLHRVFHC VLDNLVNVMN GYCLPEPYFS SKVKDWVERL
MKTLRDPSLP LLELQDIMTS VSGRIPPNVE KSIKKEMAQY ASNITSVLCQ FPSQQIANIL
DSHAATLNRK SEREVFFMNT QSIVQLVQRY RSGIRGHMKA VVMDLLRQYL KVETQFQHGH
YDKCVFALRE ENKSDMNAVL NYIFSHAQVT KKNLLVTMLI DWLCGRDPTL TDELINILTE
LTQLSKTTNA KVALRARQVL IASHLPSYEL RHNQVESIFL SAIDMYGHQF CIENLQKLIL
SETSIFDVLP NFFYHSNQVV RMAALEVYVR RAYIAYELNS VQHRQLKDNT CVVEFQFMLP
TSHPNRGNIP TLNRMSFSSN LNHYGMVHVA SVSDVLLDNS FTPPCQRMGG MVSFRTFEEF
VRIFDEVMGC FCDSPPQSPT FPEAGHTSLY DEDKSAREEP IHILNIAIKT DCDIDDDGLA
AMFRNFTQSK KSVLIDHGIR RLTFLVAQKD FRKQVNYEVD QRFHREFPKF FTFRARDKFE
EDRIYRHLEP ALAFQLELNR MRNFDLTAIP CANHKMHLYL GAAKVEVGTE VTDYRFFVRA
IIRHSDLVTK EASFEYLQNE GERLLLEAMD ELEVAFNNTN VRTDCNHIFL NFVPTVIMDP
SKIEESVRSM VMRYGSRLWK LRVLQAELKI NIRLTPTGKA IPIRLFLTNE SGYYLDISLY
KEVTDSRTAQ IMFQAYGDKQ GPLHGMLINT PYVTKDLLQS KRFQAQSLGT TYIYDIPEMF
RQSLIKLWDS MSEYALLPTL PLPSDMLTYT ELVLDDQDQE DKDDKVQGLG VEVVAAEIEK
GNAMAAWIYF RSISLPFGLL IGMVAWKITL KSPECPDGRD IIVIGNDITY RIGSFGPQED
LLFLRASELA RTEGIPRIYV AANSGARIGL AEEIRHMFHV AWEDPDDPYK GYKYLYLTPQ
DYKKVSALNS VHCEHVEDEG ESRYKITDII GKEEGLGVEN LRGSGMIAGE SSLAYEDIIT
INLVTCRAIG IGAYLVRLGQ RTIQVENSHI ILTGAGALNK VLGREVYTSN NQLGGVQIMH
NNGVTHSTVS DDFEGIYTIL QWLSYMPKSV SSPVPTLSIK DPIDRVIEFV PTKTPYDPRW
MLAGRPSPTQ KGQWLSGFFD SGSFLEIMQP WAQTVVVGRA RLGGIPVGVV AVETRTVELS
IPADPANLDS EAKIIQQAGQ VWFPDSAFKT AQAIKDFNRE GLPLMVFANW RGFSGGMKDE
ALAGTTIASA LEDDRALQQL LQRAAQGLRI QAEEVIEDVE PMVDLLALPG PACIALPLIK
TVSATTKTLW QTAASLPTTV KHNGKHYFVP LKGYEHLYCH PPPDSLVMDT ANQREQ
//
