ID A0A1L9NUA2_9RHOB Unreviewed; 398 AA.
AC A0A1L9NUA2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:OJI92782.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:OJI92782.1};
GN Name=fadA_4 {ECO:0000313|EMBL:OJI92782.1};
GN ORFNames=PFRI_29980 {ECO:0000313|EMBL:OJI92782.1};
OS Planktotalea frisia.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Planktotalea.
OX NCBI_TaxID=696762 {ECO:0000313|EMBL:OJI92782.1, ECO:0000313|Proteomes:UP000184514};
RN [1] {ECO:0000313|EMBL:OJI92782.1, ECO:0000313|Proteomes:UP000184514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH6-1 {ECO:0000313|EMBL:OJI92782.1,
RC ECO:0000313|Proteomes:UP000184514};
RA Poehlein A., Bakenhus I., Voget S., Brinkhoff T., Simon M.;
RT "Genome sequence of Planktotalea frisia SH6-1.";
RL Submitted (OCT-2016) 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:OJI92782.1}.
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DR EMBL; MLCB01000168; OJI92782.1; -; Genomic_DNA.
DR RefSeq; WP_072631514.1; NZ_QKZM01000056.1.
DR AlphaFoldDB; A0A1L9NUA2; -.
DR STRING; 696762.PFRI_29980; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000184514; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:SF22; ACETYL-COA ACETYLTRANSFERASE; 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:OJI92782.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184514};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OJI92782.1}.
FT DOMAIN 5..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..396
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 209..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 398 AA; 41960 MW; 84B1049EB8455201 CRC64;
MRDAVIVSTA RTPIGKAYRG AFNNTTPQEL AGHAIEHAVA RAGIDPARVQ DVILGAALQQ
GHSGGNIARQ AAVRAGLPVS VAGMSLDRQC ASGMMAIATA AKQVVMDGMD VAIGGGVESI
SMVQTKEMRV AADPWLMANK SDIYMSMLET AETVAERYNV RRDVQDEYAA RSQALTHAAQ
EAGRFDAEIV PLKSTMLVQD RETKEISEHE VTLAKDEGNR PSTSVESLGG LNPVFKDGMR
IKEGKYITAG NASQLSDGAS ACVIMESKAA EKAGLEPLGR YIGVMAAGCE PDEMGIGPIY
AVPPLLKAHG LTMDDIGLWE LNEAFAVQVL YSRDQLGIPD ELLNVDGGAI SIGHPYGMSG
ARMVGHALIE GKRRGAKYVV CTMCVGGGMG AAGLFEVL
//
