ID C3XCC5_OXAFO Unreviewed; 508 AA.
AC C3XCC5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EEO30851.1};
DE EC=2.8.3.- {ECO:0000313|EMBL:EEO30851.1};
GN ORFNames=OFBG_01879 {ECO:0000313|EMBL:EEO30851.1};
OS Oxalobacter formigenes OXCC13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO30851.1, ECO:0000313|Proteomes:UP000005089};
RN [1] {ECO:0000313|EMBL:EEO30851.1, ECO:0000313|Proteomes:UP000005089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO30851.1,
RC ECO:0000313|Proteomes:UP000005089};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allison M.J., Lander E., Nusbaum C., Galagan J.,
RA Birren B.;
RT "The Genome Sequence of Oxalobacter formigenes OXCC13.";
RL Submitted (FEB-2009) 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; GG658170; EEO30851.1; -; Genomic_DNA.
DR RefSeq; WP_005882359.1; NZ_GG658170.1.
DR AlphaFoldDB; C3XCC5; -.
DR STRING; 847.BRW83_0203; -.
DR GeneID; 77134112; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_019748_3_0_4; -.
DR OrthoDB; 9801795at2; -.
DR Proteomes; UP000005089; 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 Reference proteome {ECO:0000313|Proteomes:UP000005089};
KW Transferase {ECO:0000313|EMBL:EEO30851.1}.
FT DOMAIN 14..219
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 328..467
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 292
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT BINDING 382
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 406
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ SEQUENCE 508 AA; 55421 MW; D6596A8805F57A22 CRC64;
MNTDVLQKRI RLPELREKVT SPEAAAEYIK DGMKVGMSGF TLAGSVKSVP HAIVKRAATH
PLKISVVTGA SLGNDVDSAM ANAGIMSKRA PFQTDRTLRN AINRGEVMYV DNHLSETGEQ
LRKQQVKKVD VAILEAVSIT ENGEIIPTAS VGNNEIFAET ADKVIIELNL SYPLEMEGAH
DIYCATHFPT AVPINIMKPS DRAGSIGIRI PPEKIAAIVI TDEMDTPSQN LPPDAETAQI
AGHLIEFFKN EIKQGRLTES LRPLQAGIGT IANAVMSGLK TGPFKHLTMY SEVMQDSTFE
LIDAGMMDFA AATAITLSDQ KSREVFGNFA KYKDHILLRP QRISNHPEVV QRLGLITINT
ALEVDIYGHV NSTHVMGTHM MNGIGGSGDF THNAHTAIFV TKSVAKDGLI SSIVPMVPHV
DHTEHDVDIL VTEVGLADLR GLAPRERAQA IINNCVQGEY KTMLQEYVAE ANLRGGQTPH
VLEKALSWHQ RLYETGSMKD EVKLTQVA
//
