ID G3P3N9_GASAC Unreviewed; 2241 AA.
AC G3P3N9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000012212.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000012212.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000012212.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 STRING; 69293.ENSGACP00000012212; -.
DR Ensembl; ENSGACT00000012236.1; ENSGACP00000012212.1; ENSGACG00000009222.1.
DR eggNOG; KOG0368; Eukaryota.
DR GeneTree; ENSGT00940000155049; -.
DR InParanoid; G3P3N9; -.
DR OMA; TEHCKVA; -.
DR TreeFam; TF300061; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000009222; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
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:SF1; 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; PS00188; BIOTIN; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT DOMAIN 42..544
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 197..392
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1479..1809
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1813..2129
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2241 AA; 252691 MW; D395625ED7DF3FC0 CRC64;
RPSMSGLHLV KKGHNHRKMD VQRDFAVASP AEFVTRFGGN RVIEKVLIAN NGIAAVKCMR
SIRRWSYEMF RNERTIRFVV MVTPEDLKAN AENTLNADHY VPVPGGPNNN NYDNVELIVD
IAKRIPVQAV WAGWGHASEN PKLPELLDKA GVLFLGPSSK AMWALGDKVA SSIVAQSADI
PTLPWSGSGL TVAWEEDDQF QGNMISVPPE IYTKGCVRDV DDGLAWAEKI GYPVVIKASE
GGGGKGIRTV ENYEDFPSLY RQVQTEVPGS PIFIMQLAQH ARHLEVQILA DEYGNAISLF
GRDCSIQRRH QKIIEEAPAT IASPSTFEQM EQYAVRMAKM VGYVSAGTVE YLYSEDGGFH
FLELNPRLQV EHPCTEMIGD VNLPAAQLQI AMGIPLHRIK DIRLLYGETP WGDTLINFEA
PECTPSPRGH VIAARITSEN PDEGFKPSSG TVQELNFRSS KNVWGYFSVG ATGGLHEFAD
SQFGHCFSWG ENREEAISNM VVAMKELSIR GDFRTTVEYL IKLLETESFR NNDIDTSWLD
HLIAEKVQAE RPDTMLGIVC GALHVADASF QKSMSDFLHS LERGQVLPAA SLLNSVNVDL
IYEGVKFCLK VARQSPTTFV IMMNNSNIEI DVHRLSDGGL LLSYDGSSHI TYMKEEVDSY
RITVSNKTCV FEKETDPTML RSPTAGKLLH YAVDDGGHVL SGEIYAEIEV MKMVMALTVQ
QSGCVHFVKR AGAVLTPGCV VARLALDDPS SIHLVELNTA VLPPQQPLPT VGEKLHQVFH
CVLENLVKVM AGYCLEDPFF SSKLKQWVST LMKTLRDPSL PLLELQDIIT SLASRIPPSV
EKDIRKVMAQ YASNITSVLC QFPSQRIANI LDSHAATLQR KSDREVFFMN TQSIVQLVQR
YRSGIRGYMK SVVLDLLKKY LQVEIQFQQA HYDKCVINLR EQHKPDMSPV LEYIFSHAQV
SKKNILVIML IDQLCGKDSM LADELMDILN ELTQLSKMEN SKVALRARQV LIASHLPSYE
LRHNQVESIF LSAIDMYGHQ FCPENLKKLI LSETSIFDVL PNFFYHSNQV VCMAALEVYV
RRGYIAYELN SIQHQQLHDG TCAVDFQFML PSSHPNRVPV PVSGSSQFKM RRESSELFLE
GAFSPPCQRM GAMVAFQCFE DFKRNFDEVL SSFAEPLLES APFSESCPSL FEEENFKNTR
ENPIHIINVS IKNADTEDDD ALVTAFTAFA QSKRPILFEY GIRRITFLVA QKREFPKFFT
FRARDGFQED QIYRNLEPAL AFQLELNRMR NFYLTAVPCA NHKMQLYLGA ARVQEGVEVT
DYRFFIRAII RHSDLITKEA SFEYLQNEGE RLLLEAMDEL EVAFSNTGVR TDCNHIFLNF
VPTVIMDPSK IEESVRSMVM RYGSRLWKLR VMQAELKINI RLTPTGNAIP VRLFLTNESG
YYLDISLYNE VTNPSSGQIM FQSYGDKQGP LHGMLINTPY VTKDLLQAKR FQAQTLGTTY
VYDFPEMFRQ ALFKLWGPGE KYPKDVLMCT ELVVDPEGQL VQMNRLPGDN DVGMVAFKMT
MKTPEYPEGR DLVVICNDIT HMIGSFGPQE DELFLRASEL ARAEGIPRIY VAANSGARIG
LAEEVKHMFQ VAWIDPTDPY KGFKYLYLTP QDYTCVSATN SVHCRHVEEG GESRYIITDI
IGKDDGLGVE NLRGSGAIAG ETSQAYEEII TISMVTCRAI GIGAYLVRLG QRVIQVENSH
IILTGAGALN KVLGREVYAS NNQLGGIQIM HNNGVTHTTV PDDFEGVFTV LKWLSYMPKN
KHSPVPIIAT ADPVDREIEY TPTKAPYNPR WMLAGRPHPT VRGSWQSGFF DHGSFMEIME
SWAQTVVVGR ARLGGIPLGV IAVETRTVEF TVPADPANLD SESKVLQQAG QVWFPDSAFK
TAQAICDFNR EHLPLMVFAN WRGFSGGMKD MYDQILKFGA YIVDALRGFR QPVLVYIPPH
AELRGGSWVV IDPTINPLCM ELYADRESRG GVLEAEGTVE IKFRRKDLLK TMRRLDSVYA
SLVEQLASPE LPDKQGRELE TKLKAREEFL LPIYHQVAVQ FADLHDTPGR MQEKGVITDI
LEWKNVRTFF YWRLRRLLLE QVVKCEILEA NKDLSDGHMQ SMLRRWFVET EGTVKAYLWD
NNKEVVEWLE KHLTKEDGIR SGIRENIKYL KRENTLKHIR SVVEASPDIA MDCIIQMSQN
ITPSQRAKLS HLLATMDSAS T
//