ID M7MVI1_9MICC Unreviewed; 407 AA.
AC M7MVI1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=ADIAG_01689 {ECO:0000313|EMBL:EMQ98930.1};
OS Paeniglutamicibacter gangotriensis Lz1y.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paeniglutamicibacter.
OX NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ98930.1, ECO:0000313|Proteomes:UP000012015};
RN [1] {ECO:0000313|EMBL:EMQ98930.1, ECO:0000313|Proteomes:UP000012015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lz1y {ECO:0000313|EMBL:EMQ98930.1,
RC ECO:0000313|Proteomes:UP000012015};
RX PubMed=23766407;
RA Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT Station Dakshin Gangotri.";
RL Genome Announc. 1:e00347-e00313(2013).
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:EMQ98930.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOCK01000004; EMQ98930.1; -; Genomic_DNA.
DR RefSeq; WP_007270879.1; NZ_AOCK01000004.1.
DR AlphaFoldDB; M7MVI1; -.
DR STRING; 1276920.ADIAG_01689; -.
DR PATRIC; fig|1276920.7.peg.1688; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000012015; 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; IPR020613; Thiolase_CS.
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; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000012015};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 6..272
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 281..405
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 407 AA; 42103 MW; 5EB9FE1517D21B0F CRC64;
MTEAFLVGGA RTPVGRYGGA LSSVRPDDLA ALTIRAAVER AGIDPSDVDE VIFGNANGAG
EENRNVARMA WLLAGFEDTV PGITVNRLCA SGMSAITMAS HMIKAGAADI VVAGGVESMS
RAPWVMEKPD KAFAKPGASY DTSIGWRFPN PEFLSGEFSR DGKATFSMPE TAEEVARVYG
TSREDCDAFA VRSHERAIAA IEAGHFKDEI VPVTVKTRKG ETIVDTDEGP RPGTTAEVLA
KLRPVVAGGS VVTAGNASTL NDGASAIIVA SAAAIKKYGL TARARIIDGA SAGVAPEIMG
VGPVPATRKI MERSGRKIED LAAVELNEAF SSQSLASMRE LGLDPEIVNR DGGAIALGHP
LGSSGSRIVI TLLGRLEREA KDGGSKLGLA TMCVGVGQGA ALLIEGV
//