ID A0A0N0AHR0_9ACTN Unreviewed; 1085 AA.
AC A0A0N0AHR0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN ORFNames=ADK66_17500 {ECO:0000313|EMBL:KOX08164.1};
OS Micromonospora sp. NRRL B-16802.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX08164.1, ECO:0000313|Proteomes:UP000037709};
RN [1] {ECO:0000313|EMBL:KOX08164.1, ECO:0000313|Proteomes:UP000037709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX08164.1,
RC ECO:0000313|Proteomes:UP000037709};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX08164.1}.
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DR EMBL; LGEB01000064; KOX08164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0AHR0; -.
DR STRING; 1415541.ADK66_17500; -.
DR PATRIC; fig|1415541.3.peg.3663; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000037709; 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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
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; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 6..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 482..555
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 572..834
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 828..1067
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 587..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 114136 MW; 097031958B771022 CRC64;
MTVGIYPDRV LVANRGEVAV RVLRTLADLA VPSVTVYAAD DDRCLHVRRA DQAVPLPGAG
VGAYLDHNAL IEAAHAAGAT AVHPGWGFLS ENAEFARRCA EAGLVFVGPA PQVLRVLGDK
TAARAAAESA GIPVVPATGP ATFDEAAKFL AGAPEGIMIK AVAGGGGRGM RPVTDPADLA
AAFERCRSEA LGAFGDGTLY AEHLLTGRRH IEVQIVGDGT GAAVALGDRD CSLQRRRQKV
VELAPAPGLT AGLRDAVHDA AVRLAAGLGY RGVGTVEFLV GTDDFVFLEA NPRLQVEHTV
TEQVFDVDLV EIQLRLAAGA SLADIGLDGP SPKPAGTAIQ LRVTTETVRP DGGSLPATGV
LTAFDPPAGR GVRTDTHGYA GYRVGTGYDS LLAKVVVHEP GGDPSVLRRK ASRALAEFRV
EGVDTNLGVL GRLLEHPEVT DGTATTAFLD EHAAGLATAP AREPLWFPGA DVDPAAAPEP
EEGTDGIAVR APMEATVIAV PAAEGDQVTA TSVLVVLEAM KMEHQVVAGA SGVVDRLPVT
VGQTVHPGTL LASLLAGEVA ATTVDTVAEA DPDLIRPDLR RVLDRQHKTR DEARPDAVAK
RHGRGHRTAR ENLDDLCDAG TFSEYGSLVL AGQRARRSLD DLIDRTPADG LVAGVGQINR
TGCVAMAYDY TVLAGTQGYN GHRKKDRLFE LAERNRWPVV MFAEGGGGRP GDTENPGVAN
LDTRAFALLA RLSGLVPTVS VVTGKCFAGN AALVACSDFI VATPDANIGM AGPAMIEGGG
LGVYRPEEIG PTAVHAVNGV VDLVVPDDAA AVRATRQYLS YFQGRLDTWE EPDQRALRHA
VPENRRRTYD VRTVIDTLAD RDSVLELRRE HGVGMITALI RVAGRPVGLI ANNPRHLGGA
IDAEGGSKAA RFMELCDAFD LPIVSLCDTP GFMVGPAAEE SAQVRHFGRM FLAGASLTVP
MVTVVLRKGY GLGAQAMARG GFYEPELTVS WPTGEFGGMG LEGAVRLGYR KELDAVTDPD
EREALYQRLV AQMYERGSAL NIASVFEVDD VIDPAQTRNR IVGVLEAAPP PAPRSGKKRP
LVPAW
//
