ID A0A6A5EIJ5_PERFL Unreviewed; 2434 AA.
AC A0A6A5EIJ5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN ORFNames=PFLUV_G00070060 {ECO:0000313|EMBL:KAF1389111.1};
OS Perca fluviatilis (European perch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1389111.1, ECO:0000313|Proteomes:UP000465112};
RN [1] {ECO:0000313|EMBL:KAF1389111.1, ECO:0000313|Proteomes:UP000465112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:KAF1389111.1};
RA Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA Lampietro C., Guiguen Y.;
RT "A chromosome-scale genome assembly of the European perch, Perca
RT fluviatilis.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF1389111.1}.
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DR EMBL; VHII01000006; KAF1389111.1; -; Genomic_DNA.
DR OrthoDB; 14612at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000465112; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
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 FunFam; 2.40.460.10:FF:000001; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 2.40.50.100:FF:000005; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 3.30.470.20:FF:000005; Acetyl-CoA carboxylase 1; 1.
DR FunFam; 3.90.1770.10:FF:000001; acetyl-CoA carboxylase 1; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.40.50.20:FF:000005; acetyl-CoA carboxylase isoform X2; 1.
DR FunFam; 3.90.226.10:FF:000010; acetyl-CoA carboxylase isoform X2; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 2.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR005479; CPAse_ATP-bd.
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; 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:UP000465112};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..2434
FT /note="acetyl-CoA carboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025557201"
FT DOMAIN 226..728
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 382..576
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 855..929
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1671..2001
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 2005..2321
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 29..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..190
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2434 AA; 273049 MW; 24C7ACE85A93A77E CRC64;
MLPFAVLGLI LWILLLLWRI NTKAVAMPVK GEESPSGCGR PAAEEGMPAT QSPHPGEHCL
STVPTTSTHH EDNRPQASSA SVGLEVETVD TEALQASSEV NSEKPSLRAT TQRPSRTKVP
MLSSGPEARE RLKFILGASE DNSSDEEPRV TKPPSGASQP PTSAPKSSPQ QASSAVPQSS
SSGMKPSMSG LHLVNKGHKH RKMDLQRDFT VASPAEFVTR FGGNRVIDKV LIANNGIAAV
KCMRSIRRWS YEMFRNERTI RFVVMVTPED LKANAEYIKM ADHYVPVPGG SNNNNYANVE
LIVDIAKRIP VQAVWAGWGH ASENPKLPEL LDKAGISFLG PSSKAMWALG DKVASAIVAQ
SADIPTLPWT GSGLSVDWEE DDQFLGNVIS VPPEIYTKGC VLDVDDGLAG AERIGYPVVI
KASEGGGGKG IRKVESSEDF PSLFRQVQTE VPGSPIFIMQ LAQHARHLEV QILADEYGNA
ISLFGRDCSI QRRHQKIIEE APATIAAPST FEQMERCAVR LAKMVGYVSA GTVEYLYSED
GSFHFLELNP RLQVEHPCTE MIGDVNLPAA QLQIAMGIPL YRIKDIRLFY GEAPWGDTVI
NLETPDCMPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FHSSKNVWGY FSVGATGGLH
EFADSQFGHC FSWGENREEA ISNMVVAMKE LSIRGDFRTT VEYLIKLLET ESFRNNDIDT
GWLDHLIAEK VQAERPDTML GIVCGALHVA DSSFRKSMSD YLHSLERGQV LPAASLLNSV
NVELIYEGVK FCLKVARQSP TTYVIMMNGS NIEIDVHRLN DGGLLLSYVG SSHTSYMKEE
VDSYRVTVGN KTCVFEKEKD PTVLRSPSAG KLLQYMVEDG GHVNAGETYA EIEVMKMVMT
LTLQQSGCVH FVKRPGAVLQ PGCVVAHIDL DDPSSIHPVE LNTAILPPQQ PLPIVGEKLH
QVFHCVLENL VKVMDGYCLE EPLFSSKLKQ WVATLMKTLR DPSLPLLELQ EIMTSLASRI
PSSVEKDIRK VMAQYASNIT SVLCQFPSQK IANILDSHAA TLQRKADREV FFMNTQSIVQ
LVQRYRSGIR GYMKSVVLDL LTRYLQVEMQ FQQAHYDKCV INLREQHKPD MNPVLEYIFS
HAQVSKKNIL VTMLIDQLCG RDPMLADELM AIMNELTQLS KMENSKVALR ARQVLIASHL
PSYELRHNQV ESIFLSAIDM YGHQFCPENL KKLILSETSI FDVLPTFFYH SNQVVCMAAL
EVYVRRGYIA YELNSIQHHQ LQDGTCAVDF QFMLPSSHPN RGSSPTLNRV PMPVSGSSHF
QMRRQSSELF LEGALSPPCQ RMGAMVAFQC FDDFKRNFDE VLSSFAEPVL ESAPFSESCS
SLFEEENFKN TRENPIHIIN VSIKTADAED DDALVTALTA FAQSKRLVLF EYGIRRITFL
IAQKREFPKF FTFRARDGFQ EDRIYRNLEP ALAFQLELNR MRNFQMTAVP CANHKMHLYL
GAARVQEGAE VTDYRFFIRA IIRHSDLITK EASFEYLQNE GERLLLEAMD ELEVAFSNTS
VRTDCNHIFL NFVPTVIMDP SKIEESVRSM VMRYGSRLWK LRVLQAELKI NIRLTPTGNA
IPVRLFLTNE SGYYLDISLY NEVTNPSSGQ TMFESYGDKQ GPLHGMLINT PYVTKDLLQS
KRFQAQTLGT TYVYDFPEMF RQALFKLWGP GDKSPKDVLM CTELVLDHQG LLVQMNRLPG
DNDVGMVAFR MRMKTPEYPE GRDIIVICND ITHMIGSFGP QEDELFLRAS ELARAEGIPR
IYVAANSGAR IGLAEEIKHM FQVAWIDPTD PYKGFKYLYL TPQDYTRISS TNAVHCHHVE
EGGESRYIIT DVIGKEEGLG VENLRGSGTI AGESSQAYDE IITISMVTCR AIGIGAYLVR
LGQRVIQVEN SHIILTGAGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHT TVPDDFEGVF
TILQWLSYMP KNKHSPVPVI STTDPVDREI EYTPTKAPYD PRWMLAGRPH PKVRGAWQSG
FFDHGSFMEI MESWAQTVVV GRARLGGIPL GVIAVETRTV EFTVPADPAN LDSESKVLQQ
AGQVWFPDSA FKTAQAICDF NRERLPLMVF ANWRGFSGGM KDMYDQVLKF GAYIVDALRT
FHQPVLVYIP PHAELRGGSW VVIDPTINPL CMELYADRES RGGVLEAEGT VEIKFRRKDL
LKTMRRLDSV YASLVEQLAS PELSDKQSRE LESKLKAREE FLLPIYHQVA VQFVDLHDTP
GRMQEKGVIT DILDWKKVRT FFYWRLRRLL LEQVVKCEIL QATKDLGDGH MQSMLRRWFV
ETEGTVKAYL WDNNQAVVEW LEKHLTKEDG TRSRIRENIE YLKRENTLKH IRSLVQANPD
VAMDCIIHMS QNITPSQRAK LSHLLATMDS PSTS
//
