ID D4XH84_9BURK Unreviewed; 505 AA.
AC D4XH84;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EFF73774.1};
DE EC=2.8.3.- {ECO:0000313|EMBL:EFF73774.1};
GN ORFNames=HMPREF0004_4831 {ECO:0000313|EMBL:EFF73774.1};
OS Achromobacter piechaudii ATCC 43553.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF73774.1, ECO:0000313|Proteomes:UP000004510};
RN [1] {ECO:0000313|Proteomes:UP000004510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) 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:EFF73774.1}.
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DR EMBL; ADMS01000112; EFF73774.1; -; Genomic_DNA.
DR RefSeq; WP_006220974.1; NZ_GG770409.1.
DR AlphaFoldDB; D4XH84; -.
DR PATRIC; fig|742159.3.peg.315; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_019748_3_0_4; -.
DR OrthoDB; 9801795at2; -.
DR Proteomes; UP000004510; Unassembled WGS sequence.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
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 Transferase {ECO:0000313|EMBL:EFF73774.1}.
FT DOMAIN 14..215
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 323..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; 54642 MW; D710D2D78381CAB2 CRC64;
MHLDRIRHPG LLDKITSADK AALLVKDGMT VGMSGFTRAG DCKSVPAALA RRAEREPLAI
TLITGASLGH DTDKMLAQAN ALTRRMPFQV DTTLRRKINQ GDIAFIDQHL SETVEQLRAG
HLGPINVAII EAAAITETGG IVPTMSVGNS ASFARQADKI IIELNVGVPA AIEGLHDIYE
PADRPARQPI GLVSPDQRIG QPFIEVDPDK IAAIVITHEP DSPSNALPPD DETNAIAGHI
NTFLRAEVDA GRLSNALLPL QAGIGTIANA VLHGFESSDF EQLTMYSEVL QDSAIELLDQ
GKLAFASASS ITVSKPVYDK ILANLEHYRE RIVLRPQEIS NAPEIVRRLG IIAINTALEF
DIYGNVNSTH VGGTHMMNGI GGSGDFARNA HLAIFVSKSM AKNGDISSVV PMVSHVDHTE
HDVDVLVTEC GLADLRGLAP RERARAIIQH CVHPSYRAAL QDYFDRACQR GGQTPHLLEE
AFSWHQRFNE TDSMRADKPA TRKAA
//
