ID A0A171KTD0_9BURK Unreviewed; 505 AA.
AC A0A171KTD0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acetyl-CoA hydrolase {ECO:0000313|EMBL:KKO72147.1};
DE SubName: Full=Succinyl-CoA:acetate CoA-transferase {ECO:0000313|EMBL:RZS67456.1};
GN ORFNames=AAV32_07385 {ECO:0000313|EMBL:KKO72147.1}, EV679_2677
GN {ECO:0000313|EMBL:RZS67456.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO72147.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO72147.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO72147.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RZS67456.1, ECO:0000313|Proteomes:UP000292039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16618 {ECO:0000313|EMBL:RZS67456.1,
RC ECO:0000313|Proteomes:UP000292039};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000256|ARBA:ARBA00009632}.
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:KKO72147.1}.
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DR EMBL; LBNE01000003; KKO72147.1; -; Genomic_DNA.
DR EMBL; SGWZ01000004; RZS67456.1; -; Genomic_DNA.
DR RefSeq; WP_068369776.1; NZ_VZPC01000006.1.
DR AlphaFoldDB; A0A171KTD0; -.
DR STRING; 206506.AAV32_07385; -.
DR GeneID; 73002054; -.
DR PATRIC; fig|206506.3.peg.1581; -.
DR Proteomes; UP000078084; Unassembled WGS sequence.
DR Proteomes; UP000292039; Unassembled WGS sequence.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
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; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR017821; Succinate_CoA_transferase.
DR NCBIfam; TIGR03458; YgfH_subfam; 1.
DR PANTHER; PTHR43609; ACETYL-COA HYDROLASE; 1.
DR PANTHER; PTHR43609:SF1; ACETYL-COA HYDROLASE; 1.
DR Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR Pfam; PF02550; AcetylCoA_hydro; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KKO72147.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078084};
KW Transferase {ECO:0000313|EMBL:RZS67456.1}.
FT DOMAIN 11..215
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 320..463
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 288
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT BINDING 378
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 382
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 402
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ SEQUENCE 505 AA; 54905 MW; 8EDEF0B343A8C69A CRC64;
MHSDRIRLAS LKDKIVSADA AAEIFRDGMV VGMSGFTRAG DCKAVPHALA RRAARDPLSI
TLITGASLGH DTDKLLAEAG VLGRRLPFQV DTTLRRKINA GEVKFIDQHL SETVEQLRSG
FLGKLDVAVI EACAITEDGG IVPTMSVGNS ATFATMAERI IIELNTQVPA ALEGFHDIYL
PAERPNRQPV PLTDIGQRIG STSIKVDPSR IVAIVITDQP DSPSNVLPPD EETAAIAGHI
NDYLLNEVRH GRLTHSLLPL QAGIGTIANA VLHGLVDSPF HDLTMYSEVL QDSTFALLDS
GQMSFASASS ITVSKPVYEQ LIENVEKYRS RLVLRPQEIS NLPELVRRFG LITLNTALEF
DIYGNVNSTH VGGTHMMNGI GGSGDFARNA HTSIFVTKSI AKGGDISSVV PMVPHVDHSA
HDVDILVTET GLADLRGLAP RERAATIIEN CVHPLYREEL REYFRAACKR GGQTPHILEE
AFAWHTRFQQ THSMLANQEH EVAVV
//
