ID A0A218V6J5_9PASE Unreviewed; 2303 AA.
AC A0A218V6J5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetyl-CoA carboxylase 2 {ECO:0000313|EMBL:OWK61182.1};
GN Name=ACACB {ECO:0000313|EMBL:OWK61182.1};
GN ORFNames=RLOC_00014443 {ECO:0000313|EMBL:OWK61182.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK61182.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK61182.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK61182.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OWK61182.1}.
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DR EMBL; MUZQ01000045; OWK61182.1; -; Genomic_DNA.
DR STRING; 299123.ENSLSDP00000016900; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000197619; 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; 2.
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.
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 Manganese {ECO:0000256|ARBA:ARBA00023211};
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:UP000197619};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2303
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012307256"
FT DOMAIN 174..639
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 333..530
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 745..819
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1629..1870
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1874..2190
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 25..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2303 AA; 258943 MW; C1E6612548069AE3 CRC64;
MLPAALLLLA VLLLVLAKMS NARCEREKEP EESPAGPPPA ASPPGRQSPP GRPPPRAGRA
GAEQEQLAVY NPAALRRPAL AKFVLGSFDD NSSDDELMAT AFRVGRRRSS LAGVGGTVPE
PLTVSALLEP SAGIRPSMSG LDLAKRSHRK MDLQRDFSVA SPAEFVTRFG GNRVIEKVLI
ANNGIAAVKC MRSIRRWAYE MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGTN
NNNYANVELI VDISKRIPVQ AVWAGWGHAS ENHKLPELLQ KNGIAFLGPP SDAMWALGDK
VASTIVAQTL EIPTLPWSGS GLVAQWSEED QDHQQAISIP LETYAQGCVK DVEEGLEVAM
KIGYPLMIKA AEGGGGKGIR KVEGAEEFSA CFRQVQAEAP GSPIFLMQLA QHARHLEVQV
LADEYGNAIS LFSRDCSIQR RHQKIIEEAP ATIAAPAVTE MMEKVEHPCT EMVADVNLPA
AQLQIAMGIP LHRIKDIRVL YGESPWGDTP ICFHSPSNPP VPRGHVIAAR ITSENPEEGF
KPSSGTVQEL NFRSSKNVWG YFSVAAAGGL HEFADSQFGH CFSWGENREE ATSNMVVALK
ELSIRGDFRT TVEYLIKLLE TESFQNNEIH TGWLDHLIAE KVQVGVMPWG HHSPPLGGQV
LPAASLLNIV DVELLYEGVK YILQVARQSL TTYVVIMNRT HIEIDVHRLN DGGLLLSYDG
CSYTTYMKEE IDRYRITIGN KTCTFEKEKD PTVLRSPCAG KLLQYTVEDG GHVDEGKVYA
EIEVMKIIMT LAVEEAGQLH YVKRPGALLE AGCVIARLQL DDPSKVKPAQ PFTGGLPVQQ
TLPITGEKQH QVLRNVLDNL TNIMNGYCLP EPYFKTKVKE WVAQLMKTLR DPALPLLELQ
EIMTSISGRI PLAVEKSIRK VMAQYASNIT SVLCRFPSQQ IANVLDTHAA TLQRKAEREV
FFMNTQSLVQ LVQRYRSGIR GYMKAVVLDL LRRYLQVETQ FQHAHYDKCV ISLREQCKPN
MTPVLESIFS HAQVAKKNQL VIMLIDQLCG RDPTLTDELT TILHELTQLS KTEHSKVALR
ARQVLIASHM PSYELRHNQV ESIFISAIDM YGHEYCPENL KKLILSETSI FDVLPVFFYH
TNKVVRMAAL EVYVRRGYIA YELHSLQHQQ LSDGTSLVEF KFMLPSSHPN RISAPISISN
PDLARHSTEL FMDSGFSPAS QRMGVMVAFC RFEDFTRSFD EVISCFANSP SDSGLLSDAQ
ATTYDEEDTK KIREEPIHIL NIALCSADHM EDEKLVPVFR AFAQSKKNIL VDRGLRRITF
LIAQQREFPK FFTFRARDEF AEDRIYRHLE PALAFQLELS RMRNFDLTAI PCANHKMHLY
LGAARVQAGT EATDYRFFIR AIVRHSDLIT KAGWHRGASG HMRASFEYLQ NEGERLLLEA
MDELEVAFNN TIVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEV
KINIRLTPTA TAIPIRLFLT NESGYYLDIS LYKEVRDPST GNIMFQSYGD KQGPQHGMLI
NTPYVTKDLL QAKRFQAQSL GTTYVYDFPE MIRQDILTYT ELVLDSQGHL VQMNRVPGGN
ELKTPEYPKG RDIVLICNDI THKIGSFGPE EDLVFLRASE LARAEGIPRI YIAANSGARI
GFADEIKHMF QVAWVDPAEP YKGFRYLYLT PQDYTRISSM NSVRCEHVEE GGESRYVLLD
IIGKDNGFGV ENLRAAGTIA GESSRAYDEI VTISMVTCRA IGIGAYLVRL GQRVIQVENS
HIILTGVTAL NKVLGREVYT SNNQLGGVQI MHNNGVSHVT VPDDFEGVYT ILQWLSYIPK
DNQSPVPVTA ISDPVEREID FVPSKVPYDP RWMLAGRPHP TLKGTWQSGF FDQGSFMEIM
KPWAQTVVVG RARLGGLPVG VIAVETRTVE VTIPADPANL DSEAKIIQQA GQVWFPDSAF
KTAQAIRDFN REHLPLMIFA NWRGFSSGMK DMYDQMLKFG AFIVDSLRDF KQPVLVYIPP
HAELRGGSWV VIDSTINPLH VELYADKESR GGILEPGGTV EIKFRKKDLV KTMRRIDTVY
AKLVEQLGTP ELSEAQRKQL EKQLKAREEL LLPVYHQVAV RFADLHDTPG RMQEKGVITD
ILEWKSARSF LYWRLRRLLL EEMVKGEVLK ANSELSHIHI QSMLRRWFME TEGAEKGYLW
DNNQVVVEWL EKHMQEEDST QSAIRENIKY LKRDYILKHI RSLLQANPEL TIDCIVQMAQ
HITGPQKAQV AHLLSRVDTD DPS
//
