ID M7N865_9MICC Unreviewed; 412 AA.
AC M7N865;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Beta-ketoadipyl CoA thiolase {ECO:0000313|EMBL:EMQ97979.1};
GN ORFNames=ADIAG_02489 {ECO:0000313|EMBL:EMQ97979.1};
OS Paeniglutamicibacter gangotriensis Lz1y.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paeniglutamicibacter.
OX NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ97979.1, ECO:0000313|Proteomes:UP000012015};
RN [1] {ECO:0000313|EMBL:EMQ97979.1, ECO:0000313|Proteomes:UP000012015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lz1y {ECO:0000313|EMBL:EMQ97979.1,
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:EMQ97979.1}.
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; AOCK01000007; EMQ97979.1; -; Genomic_DNA.
DR RefSeq; WP_007271662.1; NZ_AOCK01000007.1.
DR AlphaFoldDB; M7N865; -.
DR STRING; 1276920.ADIAG_02489; -.
DR PATRIC; fig|1276920.7.peg.2482; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000012015; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000012015};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 17..269
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 279..401
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 105
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 412 AA; 43237 MW; D881B94A76DDF443 CRC64;
MSPQPVNTSN ARSVRDVVFV DGVRTPFGKA GEKGIYHGTR ADDLVVKCIR ELVRRNPALP
PERIDEVAIA ATTQTGDQGL TIGRTAALLA GLPQSVPGFA IDRMCAGAMT AVTTTAGSIA
FGAYDVVIAG GVEHMGNHPM GAGADPNPRF LSERIVDPAA LNMGNTAENL HDKFPAITKE
RADAYAVASQ TKLAAAYTDG NIQPDLVPVA ARRPSEGYAL HTSDEPPRPG TTLESLADLR
TPFRAHGRVT AGNAAGLNDG ATAAVLASAQ AAEELGLSVK MRLVSYAFAG VDPSIMGYGP
VPATEKALAQ AGLSIEDIGL FEINEAFAVQ VLSFLDYYGI TDEDPRVNRY GGAIAVGHPL
ASSGVRLMNQ LARQFEQDPS VRYGLTTMCI GLGMGGTVIW ENPHHADYGK DA
//
