ID A0A059LQM1_9CHLO Unreviewed; 853 AA.
AC A0A059LQM1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=acetyl-CoA carboxytransferase {ECO:0000256|ARBA:ARBA00011883};
DE EC=2.1.3.15 {ECO:0000256|ARBA:ARBA00011883};
GN ORFNames=H632_c175p0 {ECO:0000313|EMBL:KDD76578.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD76578.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD76578.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD76578.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001072};
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:KDD76578.1}.
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DR EMBL; AYPS01000175; KDD76578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LQM1; -.
DR STRING; 1291522.A0A059LQM1; -.
DR OrthoDB; 331at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000026042; Unassembled WGS sequence.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; 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 HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR NCBIfam; TIGR00513; accA; 1.
DR NCBIfam; NF041504; AccA_sub; 1.
DR PANTHER; PTHR42853; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR42853:SF3; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDD76578.1}.
FT DOMAIN 82..336
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 91786 MW; 84C0C50A19958041 CRC64;
MRSVARAAPE TVEPLSPPRP AFSRQDWLKS MMNKFNPLKR RPGNPTILDF ERPLFKVVEE
IEELKRISET HPNSEIVAAI ASLESDLESL QKETFASLTP VQRLQLARHP NRPTFLDIVY
RITDGFMQLH GDRAGYDDPA IVCGVARIGG RSVMLVGQQK GRNTRENIAR NFGMPQPYGY
RKALRFMRLA DKQGLPIVTF VDTPGAFAGL QAEELGQGEA IAVNLREMFG FSVPIISVVI
GEGGSGGALA IGCANRNLIL ENSVYYVASP EACAAILWKS RSETATATTA LRILPEHLLE
AGVMDEIVAE APGGNHFNPR GGLPIIREAV LRNLALYDEL SASEIRADRY AKFRKIGAFT
DHVTTGGDWE AALEAIRAAP GAHTAAGTWT PTQADAEYVE HMADLHERWE QTLREKREFL
NPPRTPLGRG TVVPGLAQLV ARASALREAQ GLGPPSSALP NMPGGRVLRT RDEGVTLVGT
GEEAGDGWAD AMDASSSSAP HRQSIFAKLE ARALEQLCQD MGVSLESDAL LLLRKDGEDG
GGQPGDVDAG SSEVVDSEDE SPSLVLNETT PGMAHAAAMA AARALAYRLQ HMQEAADDED
LATRDERHDG GQGTTSGAAS SSVLSPALGT AQSSADFFAL SPLERAIVQS WHDEGATRRT
STEDSGDSDA SSQSVFGPSD DADASGLGVT VVSALALAER LWQHRGELEM TEFLAAASKN
VPSDRRDAFI SHARSDPALL FRVALSLESQ RAGEELRTAQ RRMEAQEARQ RARDRREREA
LVATAPLAVR SAPSAFFSES SGDEEDIWGA EGERREEGVM RGGRVQKGAG GKAARRALEE
GDGEGAVLES LEV
//
