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Database: UniProt
Entry: Q9RM86_CLOAM
LinkDB: Q9RM86_CLOAM
Original site: Q9RM86_CLOAM 
ID   Q9RM86_CLOAM            Unreviewed;       438 AA.
AC   Q9RM86;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 2.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=4-Hydroxybutyrate CoA-transferase {ECO:0000313|EMBL:CAB60036.2};
DE   SubName: Full=Acetyl-CoA hydrolase/transferase family protein {ECO:0000313|EMBL:MBN7772164.1};
GN   Name=abfT {ECO:0000313|EMBL:CAB60036.2};
GN   ORFNames=JYB65_02205 {ECO:0000313|EMBL:MBN7772164.1};
OS   Clostridium aminobutyricum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=33953 {ECO:0000313|EMBL:CAB60036.2};
RN   [1] {ECO:0000313|EMBL:CAB60036.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSMZ 2634 {ECO:0000313|EMBL:CAB60036.2};
RX   PubMed=11041350; DOI=10.1007/s002030000195;
RA   Gerhardt A., Linder D., Huisman G., Buckel W.;
RT   "Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: cloning of
RT   two genes involved in the formation and dehydration of 4-hydroxybutyryl-
RT   CoA.";
RL   Arch. Microbiol. 174:189-199(2000).
RN   [2] {ECO:0000313|EMBL:CAB60036.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSMZ 2634 {ECO:0000313|EMBL:CAB60036.2};
RA   Lee T.-M., Wu T.-M., Sung M.-S.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007829|PDB:3GK7}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SPERMIDINE.
RX   PubMed=19804364; DOI=10.1515/bc.2009.147;
RA   Macieira S., Zhang J., Velarde M., Buckel W., Messerschmidt A.;
RT   "Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium
RT   aminobutyricum.";
RL   Biol. Chem. 390:1251-1263(2009).
RN   [4] {ECO:0007829|PDB:3QDQ}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH COENZYME A.
RX   PubMed=21833509; DOI=10.1007/s00203-011-0737-2;
RA   Macieira S., Zhang J., Buckel W., Messerschmidt A.;
RT   "Crystal structure of the complex between 4-hydroxybutyrate CoA-transferase
RT   from Clostridium aminobutyricum and CoA.";
RL   Arch. Microbiol. 194:157-166(2012).
RN   [5] {ECO:0000313|EMBL:MBN7772164.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 2634 {ECO:0000313|EMBL:MBN7772164.1};
RA   Kim Y.J., Yang J.-A.;
RT   "Abyssanaerobacter marinus gen.nov., sp., nov, anaerobic bacterium isolated
RT   from the Onnuri vent field of Indian Ocean and suggestion of
RT   Mogibacteriaceae fam. nov., and proposal of reclassification of ambiguous
RT   this family's genus member.";
RL   Submitted (FEB-2021) 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; AJ250267; CAB60036.2; -; Genomic_DNA.
DR   EMBL; JAFJZZ010000001; MBN7772164.1; -; Genomic_DNA.
DR   PDB; 3GK7; X-ray; 1.85 A; A/B=1-438.
DR   PDB; 3QDQ; X-ray; 2.60 A; A=1-438.
DR   PDBsum; 3GK7; -.
DR   PDBsum; 3QDQ; -.
DR   KEGG; ag:CAB60036; -.
DR   BioCyc; MetaCyc:MONOMER-13484; -.
DR   Proteomes; UP000664545; 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   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   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   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3GK7, ECO:0007829|PDB:3QDQ};
KW   Hydrolase {ECO:0000313|EMBL:MBN7772164.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000664545};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAB60036.2}.
FT   DOMAIN          7..178
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          272..429
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   BINDING         216
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0007829|PDB:3QDQ"
FT   BINDING         218
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0007829|PDB:3QDQ"
FT   BINDING         238
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0007829|PDB:3QDQ"
FT   BINDING         313
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0007829|PDB:3QDQ"
FT   BINDING         332
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0007829|PDB:3QDQ"
FT   BINDING         337
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0007829|PDB:3QDQ"
FT   BINDING         372
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0007829|PDB:3QDQ"
SQ   SEQUENCE   438 AA;  47697 MW;  BFBD3241C20FFE73 CRC64;
     MDWKKIYEDR TCTADEAVKS IKSGDRVLFA HCVAEPPVLV EAMVANAAAY KNVTVSHMVT
     LGKGEYSKPE YKENFTFEGW FTSPSTRGSI AEGHGQFVPV FFHEVPSLIR KDIFHVDVFM
     VMVSPPDHNG FCCVGVSSDY TMQAIKSAKI VLAEVNDQVP VVYGDTFVHV SEIDKFVETS
     HPLPEIGLPK IGEVEAAIGK HCASLIEDGS TLQLGIGAIP DAVLSQLKDK KHLGIHSEMI
     SDGVVDLYEA GVIDCSQKSI DKGKMAITFL MGTKRLYDFA ANNPKVELKP VDYINHPSVV
     AQCSKMVCIN ACLQVDFMGQ IVSDSIGTKQ FSGVGGQVDF VRGASMSIDG KGKAIIAMPS
     VAKKKDGSMI SKIVPFIDHG AAVTTSRNDA DYVVTEYGIA EMKGKSLQDR ARALINIAHP
     DFKDELKAEF EKRFNAAF
//
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