ID A0A0K2G6M4_NITMO Unreviewed; 398 AA.
AC A0A0K2G6M4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ALA56499.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ALA56499.1};
GN Name=atoB {ECO:0000313|EMBL:ALA56499.1};
GN ORFNames=NITMOv2_0057 {ECO:0000313|EMBL:ALA56499.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA56499.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA56499.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA56499.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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; CP011801; ALA56499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K2G6M4; -.
DR STRING; 42253.NITMOv2_0057; -.
DR KEGG; nmv:NITMOv2_0057; -.
DR PATRIC; fig|42253.5.peg.59; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000069205; Chromosome.
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; IPR020610; Thiolase_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.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ALA56499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ALA56499.1}.
FT DOMAIN 8..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..394
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 398 AA; 41364 MW; 113617AFAC39CF74 CRC64;
MSAPQTSVIV SAVRTPMGAF NGAFSAVPAT KLGSLAIAEA LKRIHLPADR VEAVYMGCAI
SAGLGQAPAR QASIGAGIPC SVGAVTVNKV CGSSIQTVIM AAQAIALGEA GIVVAGGMEN
MTCAPYLLEK ARQGYRLGHA ELVDSLIKDG LWDVYNDFHM GDGGELCAAK YRLTRREVDD
FALESYRRAR EAIATGAFKP EIVPVEVPQR KGPPVTVVDD EEPNRVDLKK MRDLKPAFQE
NGILTVGNSP SCNDGAAALV VMAEAEAARL GLAPLARIVG YAGAALAPEW FTIAPVEAIK
LVLKKTGLTI GDIDLFEINE AFSAVSLAIN RELGLDTKKV NVNGGAVALG HPIGATGARI
LTTLVHAMNA RGARRGLASL CIGGGEALAI IVERGYAG
//
