ID F5XEV7_MICPN Unreviewed; 400 AA.
AC F5XEV7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Putative fatty acid oxidation complex beta subunit {ECO:0000313|EMBL:BAK35323.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:BAK35323.1};
GN OrderedLocusNames=MLP_23090 {ECO:0000313|EMBL:BAK35323.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK35323.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK35323.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; AP012204; BAK35323.1; -; Genomic_DNA.
DR RefSeq; WP_013863195.1; NC_015635.1.
DR AlphaFoldDB; F5XEV7; -.
DR STRING; 1032480.MLP_23090; -.
DR KEGG; mph:MLP_23090; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_11; -.
DR OrthoDB; 4440515at2; -.
DR Proteomes; UP000007947; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase 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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:BAK35323.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007947};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:BAK35323.1}.
FT DOMAIN 8..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 94
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 400 AA; 42098 MW; D866AA5AB8E8F2A3 CRC64;
MPRQSRDVVF VDGVRTPFGK AGSLYSETRA DDLVVSCIRA LLRRHPELPP ERVDEVAIAA
TTQTGDQGLT IGRTAALLAG LPRSVPGYAI DRMCAGAMTA VTTTASGIAF GAYDVTIAGG
VEHMGRHPMG EGIDPNPRIV AERLVDPSAL VMGSTAENLH DRFPGISRQR ADEFAAQSQQ
RVASAYAQGV IQESLVPIAT RSAELGWGLA TADEPPRPGT TVEALAQLRT PFRSHGRVTA
GNAAGLNDGA TACLLAAESV AEELGLPAAM RLVSYGFAGV EPEVMGVGPI PSTEKALRSA
GLEMSDIGAI EINEAFAVQV LAFLDHFGLD PASDRINPYG GAIALGHPLA SSGVRLMIHL
ARQFREHPEI RYGLTTMCIG LGMGGTLIWE NPHHTEGADK
//
