ID C3PIV7_CORA7 Unreviewed; 432 AA.
AC C3PIV7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Acyl-CoA thiolase {ECO:0000313|EMBL:ACP33761.1};
GN Name=fadA2 {ECO:0000313|EMBL:ACP33761.1};
GN OrderedLocusNames=cauri_2168 {ECO:0000313|EMBL:ACP33761.1};
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP33761.1, ECO:0000313|Proteomes:UP000002077};
RN [1] {ECO:0000313|EMBL:ACP33761.1, ECO:0000313|Proteomes:UP000002077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC {ECO:0000313|Proteomes:UP000002077};
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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; CP001601; ACP33761.1; -; Genomic_DNA.
DR RefSeq; WP_010188980.1; NZ_ACLH01000052.1.
DR AlphaFoldDB; C3PIV7; -.
DR STRING; 548476.cauri_2168; -.
DR GeneID; 31924822; -.
DR KEGG; car:cauri_2168; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_11; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000002077; Chromosome.
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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000002077};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 8..282
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 307..432
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 155..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 432 AA; 45787 MW; EB4961F39FDDE8A7 CRC64;
MTNPPHRVAI LGGNRIPFAR SNTQYAHASN QDMLTSALDG LVARYGLHDE RLGLVAAGAV
LKHSRDFNLT RESVLGSALD STTPAIDVQQ ACCTSLAAAI HVGDAIAQGR ISAGIAGGTD
TTSDAPLAVN DTLRRTLLNL TRAKTAAQRA QLVGSIRPSQ LAPEQPQNGE PRTGLSMGDH
AAITAREMNV SREAQDELAL ASHQNLHKAW EEGFFDDLTT GFLGVNRDTN LRPDSSLESL
AKLKAVFGKR DAEQHGAQAT MTAGNSTPLT DGASVALLSS EEWAVEHNIE PRAFLLDSET
AAVDFVHGPD GLLMAPTYAV PRLLERNNLS LQDFDFYEIH EAFASQVLAT LSAWEDETYC
RERLGLQSAL GSIDRAKLNV KGSSLAAGHP FAATGTRILA TTAKILEENG GGRALISICA
AGGQGVAAIV ER
//
