ID X5EBJ1_9CORY Unreviewed; 428 AA.
AC X5EBJ1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AHW64755.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:AHW64755.1};
GN Name=phbA {ECO:0000313|EMBL:AHW64755.1};
GN ORFNames=CGLY_11550 {ECO:0000313|EMBL:AHW64755.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW64755.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW64755.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW64755.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP006842; AHW64755.1; -; Genomic_DNA.
DR RefSeq; WP_052540119.1; NZ_CP006842.1.
DR AlphaFoldDB; X5EBJ1; -.
DR STRING; 1404245.CGLY_11550; -.
DR KEGG; cgy:CGLY_11550; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_11; -.
DR OrthoDB; 4475716at2; -.
DR Proteomes; UP000023703; Chromosome.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:AHW64755.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023703};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AHW64755.1}.
FT DOMAIN 18..286
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 295..424
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 226..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 412
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 428 AA; 43936 MW; B01E1A052D41FFE6 CRC64;
MNDTPTSTPT TAPAPTDVVL CSPLRTPVGA YGGAFTDVPV QELASTVVSA IVERTGLTAD
SIDDIILGQA SPDGAAPALG RVVALDSGLG DSVPGMQLDR RCGSGLQAVV TAAAHVATGA
ADLIIAGGAE SMSRTGYSVD GSIRWGVKGG DLVLHDRLAE GRASAGGRHH PIPGGMIETA
ENLRREYGIT REAQDALAAE SHRRAVAAID DGLFADEIVP VTVPGKRRRD PETVVDRDEH
PRPGTTTEKL AGLRPVMGRQ DDEATVTAGN ASGQNDGAAA MVVTTRARAE ELGLEPFARL
SGWAVAGVAP ETMGIGPVPA TARVLDRLGI TLDDLDVIEL NEAFAAQALS VLQEWGVPAD
DPRLNPHGSG ISLGHPVGAT GARMLVTLCH ELRRRGKDGD GTDGLRGLAT MCIGGGQGLA
AVLEAEQA
//
