ID M1YZJ0_NITG3 Unreviewed; 392 AA.
AC M1YZJ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:CCQ90655.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:CCQ90655.1};
GN Name=atoB {ECO:0000313|EMBL:CCQ90655.1};
GN ORFNames=NITGR_330053 {ECO:0000313|EMBL:CCQ90655.1};
OS Nitrospina gracilis (strain 3/211).
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Nitrospina.
OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ90655.1, ECO:0000313|Proteomes:UP000011704};
RN [1] {ECO:0000313|EMBL:CCQ90655.1, ECO:0000313|Proteomes:UP000011704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ90655.1,
RC ECO:0000313|Proteomes:UP000011704};
RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT of the major marine nitrite oxidizer.";
RL Front. Microbiol. 4:27-27(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:CCQ90655.1}.
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DR EMBL; CAQJ01000037; CCQ90655.1; -; Genomic_DNA.
DR RefSeq; WP_005008424.1; NZ_HG422173.1.
DR AlphaFoldDB; M1YZJ0; -.
DR STRING; 1266370.NITGR_330053; -.
DR HOGENOM; CLU_031026_0_1_0; -.
DR InParanoid; M1YZJ0; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000011704; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:CCQ90655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011704};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CCQ90655.1}.
FT DOMAIN 9..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 348
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 392 AA; 41921 MW; A1BABAF8ED31D55E CRC64;
MSRENSFTYI YSAVRTPIGR FNGALAPVPA PELAAFAIRE ALKRGGFEGE DIDEVILGNV
LTAGVGQAPA RQAALHSGIP DNVGATTVNK VCGSGMKAVM MADQSIRLSQ SDFVVAGGME
NMSRAPFLVP HMRRGHKLGN AHMVDGMIHD GLWDPHENRH MGELSQILAH RLGYTREAQD
AYAKESYTRA RKAMDKGIVA KELVTIPVWH RTYTQTVDHD EQPHLDNLDQ FDSMPPVFEK
PGGTITKANG AKLSDGAAAL IVGKPSANHK PLARILGYAA HAQSPDTFAL APVEAIRKVL
AAVRLEIKDI DLFEINEAFA PMSLAVNDQL GLDPEKVNVH GGSIALGHPI GATGARILVT
LLNALKTQGK RRGCASLCIG GGEATAMVIE LV
//
