ID Q0RWG8_RHOJR Unreviewed; 719 AA.
AC Q0RWG8;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Acetyl-CoA hydrolase/transferase {ECO:0000313|EMBL:ABH00368.1};
DE EC=3.1.2.1 {ECO:0000313|EMBL:ABH00368.1};
GN OrderedLocusNames=RHA1_ro10175 {ECO:0000313|EMBL:ABH00368.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL2 {ECO:0000313|EMBL:ABH00368.1,
OG ECO:0000313|Proteomes:UP000008710}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABH00368.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000256|ARBA:ARBA00009632}.
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DR EMBL; CP000433; ABH00368.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0RWG8; -.
DR KEGG; rha:RHA1_ro10175; -.
DR HOGENOM; CLU_019748_3_1_11; -.
DR Proteomes; UP000008710; Plasmid pRHL2.
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:ABH00368.1};
KW Plasmid {ECO:0000313|EMBL:ABH00368.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Transferase {ECO:0000313|EMBL:ABH00368.1}.
FT DOMAIN 223..388
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 538..684
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT REGION 70..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 509
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT BINDING 484..488
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 599
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 603
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 623
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ SEQUENCE 719 AA; 76577 MW; D2035D76CD1A88E5 CRC64;
MRSSINCRRG SQESPISPAE LFSLGTDRSH MAVLAGSRVP VHASGHPGPR SSGCRGRATY
PRVVAARSLA HGAQPDSRGP APDVPRWPGG GHRIADRRDV SGTVRCCHRH SGDGPLSGGQ
ESRPVGVMCA RLSPGKLGGV SRITLRGAFG RDSTGDLTEP TSGGPAATNG RGRRAVANTE
CDPVNITTFR GVHVTSPTPT LAAVSLQISD PASPVQSSRI RHSALQQKVT SAEEAVKAIG
PGDTVAVSGF ASAGTPKAVI PALADRIHAA RAAGANFTID LLTGASVSTE TERMLTEIDG
IALRMPYQAE STARQKINQG RMDYVDIHLS HVAQQVWEGY YGAVNVAVVE VSGITETGEL
IPSASVGNNK TWLDVAEKVI LEVNSWVPDA MDGIHDIYYG TALPPHRRPI ELTDVEDRIG
QPHYRVDPAK VVAVVQTNAP DSASALTAPD AVSEAIAAHV LDFFDHEVKC GRLPENTLLP
LQAGIGNVAN AVLGGLERGP YRGLTCYSEV IQDGMLHLIK HGTVRFASAT ALALSEAGIE
ELTSNIDFYR QHIRLRPQEI SNHPEVVRRL GIIAMNGMLE ADIYGNVNST HVMGTKIMNG
IGGSGDFARN GYLSMFLSPS TAKNGAISSI VPMTPHVDHT EHDTQVLVTE QGLADLRGLS
PRRRARVIIE RCAHPEFRPL LTDYIERATA TAGAGQTPHL LGEAFSFHQR YLESGSMRV
//
