ID A0A0F3GQU3_9BACT Unreviewed; 428 AA.
AC A0A0F3GQU3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KJU84270.1};
GN ORFNames=MBAV_003526 {ECO:0000313|EMBL:KJU84270.1};
OS Candidatus Magnetobacterium bavaricum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetobacterium.
OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU84270.1, ECO:0000313|Proteomes:UP000033423};
RN [1] {ECO:0000313|EMBL:KJU84270.1, ECO:0000313|Proteomes:UP000033423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU84270.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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:KJU84270.1}.
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DR EMBL; LACI01001545; KJU84270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3GQU3; -.
DR PATRIC; fig|29290.4.peg.4688; -.
DR Proteomes; UP000033423; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 2.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 2.
DR SUPFAM; SSF53901; Thiolase-like; 3.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000033423};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KJU84270.1}.
FT DOMAIN 4..45
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 76..298
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 307..428
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 123
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 415
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 428 AA; 45686 MW; 0C48FAFA3A4B90AA CRC64;
MKEVVIVSGV RTAVGAFGGV LKDVSAIDLG ALVIKETLKK VGLRPVVDEA LKEFAPDKLK
DQGMIELEKR YHDYDSALKP VSIDEVVMGN VVQAGQGQNP ARQATIKSGI PKETPAATIN
KVCSSGLRSI AMGVQSIMLG EADVVVAGGM ESMSNIPFTL PSARWGYRMA LTGVADVIDL
MVYDGLYEIF YGYHMGITAE NIVQLYGITR EEQDQLSVLS HTRARQAITD GTFKEEIVPV
VIKGRKEDII VDTDERPMDT SMEKLGKMKP AFKKDGSVTA GNASGINDGA AAVLLMSADK
AKAMGLEPYV KIKGFATGAI DPAYMGLGPI PAVRKLLKQH GLGVGDIDCW EVNEAFAAQA
LACIKELGLA SDKPNELGSG ISLGHPIGCT GARQVVTGMR QMKRKGYKRG IVTMCIGGGM
GYAMLMER
//
