ID G5GQM9_9FIRM Unreviewed; 498 AA.
AC G5GQM9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHG20664.1};
GN ORFNames=HMPREF9334_01560 {ECO:0000313|EMBL:EHG20664.1};
OS Selenomonas infelix ATCC 43532.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=679201 {ECO:0000313|EMBL:EHG20664.1, ECO:0000313|Proteomes:UP000004129};
RN [1] {ECO:0000313|EMBL:EHG20664.1, ECO:0000313|Proteomes:UP000004129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43532 {ECO:0000313|EMBL:EHG20664.1,
RC ECO:0000313|Proteomes:UP000004129};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas infelix ATCC 43532.";
RL Submitted (AUG-2011) 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:EHG20664.1}.
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DR EMBL; ACZM01000015; EHG20664.1; -; Genomic_DNA.
DR RefSeq; WP_006692996.1; NZ_JH376799.1.
DR AlphaFoldDB; G5GQM9; -.
DR STRING; 679201.HMPREF9334_01560; -.
DR PATRIC; fig|679201.3.peg.1576; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_019748_3_0_9; -.
DR OrthoDB; 9801795at2; -.
DR Proteomes; UP000004129; 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;
FT DOMAIN 12..202
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 317..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 263..267
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 358
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
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 498 AA; 54070 MW; A237FB24341845DD CRC64;
MIDISDRIPK SLADKVVSAE TAAEYFADGM TIGASGFTPS GYPKAVTLAI AERMKKNPFK
VNIWTGASTG PELDGALAEA GGIKQRLPYQ TNTPLRNAIN SGLVNYIDMH LSEVAQQSRE
GFLGKIDVAL VEAVAITEEG IIPSTSVGNT PSFIQSADVV IVEVNTSQPM ELVGMHDIYI
PLDPPNRLPI PITKAGDRIG TTFMPCPLEK IKYIVPCDIT DKTRALAPVD DIARKMGQFT
VDLLKKEIAE GRMPKGLLPL QSGVGNVANA VIAGFVSSDF TDLEVYTEVI QDGMFDLADA
GKLKFASGTA FSPSPEGLQR FYKDIDKYKK IMMLRPQEIS NNPEVVRRLG VIAMNTAIEV
DIYGNVNSTH VTGTKMMNGI GGSGDFARNA YLTIFYTQSE AKGGKISSIV PFCSHIDHGA
HDVDIVITEQ GVADLRGKSP RERAHEIINN CAHPDYRPLL LDYYERAYAA TKGAQTPHLL
DEALSFHQRF LATGSMQK
//
