ID A0A452R4U2_URSAM Unreviewed; 1942 AA.
AC A0A452R4U2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetyl-CoA carboxylase beta {ECO:0000313|Ensembl:ENSUAMP00000013461.1};
GN Name=ACACB {ECO:0000313|Ensembl:ENSUAMP00000013461.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000013461.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000013461.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSUAMT00000015092.1; ENSUAMP00000013461.1; ENSUAMG00000009444.1.
DR GeneTree; ENSGT00940000155049; -.
DR Proteomes; UP000291022; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 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; 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; IPR011054; Rudment_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; 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; 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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022}.
FT DOMAIN 1..270
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 60..118
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1206..1536
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1540..1829
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1942 AA; 219296 MW; DFFF2B25AC53FE65 CRC64;
MKLAEHARHL EVQILADQYG NAVSLFGRDC SIQRRHQKII EEAPATIAIP VVFEIMEQCA
VRLAKTVGYV STGTVEYLYS QDGSFHFLEL NPRLQVEHPC TEMIADVNLP AAQLQIAMGV
PLHRLKDIRL LYGESPWGVT PISFDTPANP PLARGHVIAA RITSENPDEG FKPSSGTVQE
LNFRSNKNVW GYFSVAAAGG LHEFADSQFG HCFSWGENRE EAISNMVVAL KELSIRGDFR
TTVEYLINLL ETERFQNNDI DTGWLDYLIA EKVQAEKPDI MLGVVCGALN VADAMFRTCM
TDFLHSLERG QVLPAASLLN IVDVELIYGG VKYILKVARQ SLTMFVLIMN DCHIEIDAHR
LSDGGLLLSY NGNSYTTYMK EEFDSYRITI GNKTCVFEKE NDPTVLRAPS AGKLLQYTVE
DGGHVEAGSS YADMEVSAEP VLGVGPQPGL PSIPLPGGGP SRIAPAKPFT GELPSQQTLP
IVGEKLHQVF HNVLENLTNV MSGFCLPEPI FSTKLKEWVQ KLMMTLRHPS LPLLELQEIM
TSVSGRIPAP VEKSVRRVMA QYASNITSVL CQFPSQQIAT ILDCHAATLQ RRAEREVFFM
NTQSIVQLVQ RYRSGTRGYM KAVVLDLLRR YLRVEHHFQQ AHYDKCVINL RERLKPDMSQ
VLDCIFSHAQ VAKKNQLVIM LIDELCGPDP SLSEELTSIL NELTQLSKSE HCKVALRARQ
VLIASHLPSY ELRHNQVESI FLSAIDMYGH QFCPENLKKL ILSETTIFDV LPTFFYHANK
VVCMASLEVY VRRGYIAYEL NSLQHRQLPD GTCVVEFQFM LPSSHPNRYG VVRTQGRCVF
LFSRTPIVLL FMDSGFSPLC QRMGAMVAFR RFEDFIRYPE WPSLSNTPSR GGWGPRVLLP
PAFVLLSQNP REEPIHILNV ALQYADHLED EELVPIFRKF VQSKVLLTPR TPGVCKTGRG
PSRHAAPVSH SVSVYLSVCL RSLAGPQFAE DRIYRHLEPA LAFQLELSRM RSFDLTAVPC
ANHKMHLYLG AAKVKEGAEV TDHRFFIRAI IRHSDLVTKE ASFEYLQNEG ERLLLEAMDE
LEVAFNNTSV RTDCNHIFLN FVPTVIMDPS KIEESVRSMV MRYGSRLWKL RVLQAEVKIN
IRQTTTGSAV PIRLFITNES GYYLDISLYK EVTDPRSGNV RGKKDIMFHS FGNKQGPQHG
MLINTPYVTK DLLQAKRFQA QSLGTTYVYD FPELFRQALF KLWGTPDKYP KDILTYTELV
LDPQGQLVEM NRLPGGNEVG MVAFKMRFKT PEYPEGRDVI VISNDITFRI GSFGMGEDLL
YLRASEMARA EGIPKIYLAA NSGACIGLAE EIKHIFQVAW VDPGDPHKGL KYLYLTPQDY
TTISSLNSVH CRHIEEDGES RYVITDIIGK DSGVGIENLR GSGMIAGESS LAYDEIVTIS
LVTCRAVGIG AYLVRLGQRV IQVENSHIIL TGVSALNKVL GREVYTSNNQ LGGVQIMHYN
GISHITVPDD FEGVCTILEW LSYMPKDNHS PVPIITPTDP IDREIGFFPT RAPYDPRWLL
AGRPHPTLKG SWQSGFFDHG SFKEIMAPWA QTVVTGRARH RDSQIIQQAG QVWLPDSAYK
TAQAIKDFNR ERLPLMIFAN WRGFSGGMKD MYDQMLKFGA YIVDSLRQYK QPVLIYIPPS
AELRGGSWVV VDSSINPLCI EMYADKESRA NILEPEGTVE IKYRKKDLIK TMRRIDPAYK
KLVEQLGMSG LSDKDRKDLE GQLKAREDLL LPIYHQVAVQ FADLHDSPTC LLEKGAISDI
LEWKTARSFL YWRLRRLLLE DQVKQEILRA SGELSHVHIQ SMLRRWFVET EGAVKAYLWD
NNQMVVQWLE QHWQGEDSLR STVRENIRCL KRDSVLKAIR GLVQDNPEVA VDCIVYMSQH
ISPAERAQVI HLLSTMDSAA ST
//
