ID A0A1Q7TJF3_9BACT Unreviewed; 276 AA.
AC A0A1Q7TJF3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JUN-2023, entry version 24.
DE RecName: Full=acetyl-CoA carboxytransferase {ECO:0000256|ARBA:ARBA00011883};
DE EC=2.1.3.15 {ECO:0000256|ARBA:ARBA00011883};
GN ORFNames=AUG81_06040 {ECO:0000313|EMBL:OLD88635.1};
OS Verrucomicrobia bacterium 13_1_20CM_4_54_11.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=1805408 {ECO:0000313|EMBL:OLD88635.1, ECO:0000313|Proteomes:UP000185599};
RN [1] {ECO:0000313|EMBL:OLD88635.1, ECO:0000313|Proteomes:UP000185599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD88635.1}.
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DR EMBL; MNIL01000070; OLD88635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7TJF3; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000185599; 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 InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
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; 2.
PE 4: Predicted;
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..159
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT DOMAIN 160..242
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 276 AA; 31657 MW; 7B1CFFFD2A5C51A5 CRC64;
MKEPQPLDFE KPIMELQRRL QEIRDHSDEH ALDFDAEVEA MEAKIETTRR EIYGNLSAWQ
RVQIARHTQR PFALDYVERC FTNWNELHGD RLFGDDKAMP CGIAMLGEQR CVVITNQKGR
NTKENVMRNF GCAHPEGYRK ALRLMQLGEK FNLPVISLVA DHVMILENAY YSVISPEACS
AILWKDRRHA AEAAEALKLT GQDLMKLNVV DEVVAEPDGG AHRDHEKAAQ ILREALRSNL
KRLLKTPINQ LLKKRYEKFR RLGNFAEPPR GNGATG
//
