ID Q5QVV4_IDILO Unreviewed; 613 AA.
AC Q5QVV4;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=4-Hydroxybutyrate CoA-transferase (N-terminal) fused to acetyltransferase (C-terminal) domain of GNAT superfamily {ECO:0000313|EMBL:AAV83129.1};
GN OrderedLocusNames=IL2297 {ECO:0000313|EMBL:AAV83129.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV83129.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV83129.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000256|ARBA:ARBA00009632}.
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DR EMBL; AE017340; AAV83129.1; -; Genomic_DNA.
DR RefSeq; WP_011235523.1; NC_006512.1.
DR AlphaFoldDB; Q5QVV4; -.
DR STRING; 283942.IL2297; -.
DR KEGG; ilo:IL2297; -.
DR eggNOG; COG0427; Bacteria.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_030703_1_0_6; -.
DR OrthoDB; 9801795at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.750.70; 4-hydroxybutyrate coenzyme like domains; 1.
DR Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1.
DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR InterPro; IPR026888; AcetylCoA_hyd_C.
DR InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR InterPro; IPR046433; ActCoA_hydro.
DR InterPro; IPR003702; ActCoA_hydro_N.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR21432:SF20; ACETYL-COA HYDROLASE; 1.
DR PANTHER; PTHR21432; ACETYL-COA HYDROLASE-RELATED; 1.
DR Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR Pfam; PF02550; AcetylCoA_hydro; 1.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001171};
KW Transferase {ECO:0000313|EMBL:AAV83129.1}.
FT DOMAIN 454..609
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 613 AA; 68251 MW; BB5A9752527D8DF6 CRC64;
MTKTKLDWSK ILKSGQRIFI GSHAAVPTAL IDDLIENSKN LHDIEIVQLM TLSDNKWAGP
QYQQLFKVNT FFIGGDTVRT AVNEGRADYT PSFISDIPNL FSNGILPLDA ALIMVSPADK
YGYHSMGVSV DVVAAAAKSA NTVIAQVNPN MPVTYGQSFL HTNQIHHFWE HAAPLPELPP
PSLENNKIIE RIGQYIALLV ENGATLQIGV GTICAAALRY LSNHKDLGIH SELITDDVMH
LMLKGVINNR KKTFHPNKIV TSFCMGSKAL YDFVDHNPHV GFYPSEYVNS PANVARNDKL
VAINSAIEVD LTGQIVSDSI GHQFYSGIGG QVDFSRGASL SKGGKPVIAL PSTTEDGKVS
RIVPFIREGA GVVTTRGHVH YVVTEFGVAS LRGKSIRERA LELIRVAHPK FRSHLLQEVR
KHYWVPNYQQ QTPVDVPELG DIGFKKLKIN NESFDLRPLY PSDERRLQEF FYSHTKETLQ
LRYNAVPTNM TREKSCNLVS VDQSRDLALC IVRQKGSAVQ IQAVGRYYFI ESQNSCEVAF
VTREKYQGRG MAGMLLDEMI RIAKERKLDS MQAYVLAANK PMLSVFERGG FKRLPSEEPG
EVLLKLELNE DAD
//
