ID Q13EC9_RHOPS Unreviewed; 520 AA.
AC Q13EC9;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Acetyl-CoA hydrolase {ECO:0000313|EMBL:ABE37560.1};
DE EC=3.1.2.1 {ECO:0000313|EMBL:ABE37560.1};
GN OrderedLocusNames=RPD_0322 {ECO:0000313|EMBL:ABE37560.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37560.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE37560.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE37560.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000256|ARBA:ARBA00009632}.
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DR EMBL; CP000283; ABE37560.1; -; Genomic_DNA.
DR AlphaFoldDB; Q13EC9; -.
DR STRING; 316057.RPD_0322; -.
DR KEGG; rpd:RPD_0322; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_019748_3_0_5; -.
DR BioCyc; RPAL316057:RPD_RS01635-MONOMER; -.
DR Proteomes; UP000001818; Chromosome.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
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:ABE37560.1}.
FT DOMAIN 17..224
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 325..471
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 296
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT BINDING 271..275
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 366
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 386
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 390
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 410
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ SEQUENCE 520 AA; 56861 MW; E31F1A82A90E19FC CRC64;
MVASASRVLD PHLRSRIMTA ADAAALIPSG ANVGMSGFTG SGYPKLLPLA LAERINAHHA
RGQKFKVSVW TGASTAPELD GALAKVDGIE MRLPYQSDPT CRKRINAGRM EYIDIHLSHV
AQHVWFGFLG KLDVAIVEVA GIREDGSLIP SSSIGNNKTW LDLADKVILE VNAWQDIRLE
GMHDVYYGTQ LPPHRKPIPI VASGDRIGEQ YLRCDPSKIV AIVETNLPDR NSAFSAPDEA
SQAIAEHILE FLGHEVKKGR LPPNLLPLQS GVGNVANAVM AGLEDGPFDN MTAYTEVLQD
GMLSLLRKGK LAHASATALS LSPDGYDEFL RNLDFYRERI LLRPQEISNH PEVIRRLGVI
AMNGLIEADI YGNVNSTHIT GTSIMNGIGG SGDFARNSYL SFFMTPSAAK GGKISCIVPM
ASHVDHTEHD VQVIVTEQGL ADLRGLSPKQ RAKVIIQNCA HPTFKPALKE YYKRALEYSP
GLHTPHILDE ALTFLPNWMA NKAAREAWRE DAVVQADVWR
//
