ID N9CXQ0_ACIBZ Unreviewed; 506 AA.
AC N9CXQ0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ENV90637.1};
GN ORFNames=F938_03886 {ECO:0000313|EMBL:ENV90637.1};
OS Acinetobacter bereziniae LMG 1003 = CIP 70.12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=981324 {ECO:0000313|EMBL:ENV90637.1, ECO:0000313|Proteomes:UP000013251};
RN [1] {ECO:0000313|EMBL:ENV90637.1, ECO:0000313|Proteomes:UP000013251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 70.12 {ECO:0000313|EMBL:ENV90637.1,
RC ECO:0000313|Proteomes:UP000013251};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter bereziniae CIP 70.12.";
RL Submitted (FEB-2013) 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:ENV90637.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APQG01000049; ENV90637.1; -; Genomic_DNA.
DR RefSeq; WP_005034391.1; NZ_KB849756.1.
DR AlphaFoldDB; N9CXQ0; -.
DR PATRIC; fig|1217650.3.peg.3821; -.
DR HOGENOM; CLU_019748_3_0_6; -.
DR OrthoDB; 9801795at2; -.
DR Proteomes; UP000013251; 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 11..215
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 321..464
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 289
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT BINDING 379
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 383
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 403
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ SEQUENCE 506 AA; 55197 MW; 98511C8202E14CCA CRC64;
MSLDRIRLAS LHDKVMSAEQ AATFIQDGMT VGMSGFTRAG EAKAVPLALV KQAKVNPLKI
TLITGASLGN DLDKQLTEAG VLARRLPFQV DNTLRKAINK GEVMFIDQHL SETVEQMRNL
QLKKPDVAVI EAIAITEDGG IIPTTSVGNS ASFAIFAEKV IVEINTNLSP AFEGLHDIYI
PTYRPTRQPI PLTHVDQRIG TPAINIDPTK IVGIVINSEF HDSPSTVTLP DDETQSIANH
LIAFFEKEVE EGRLPANLGP LQAGIGSIAN AVLTGLKESN FEDLVMYSEV LQDCTFELID
AGKMKFASGS SITLSAKYGE KVFNNLEQYK DKLVLRPQEI SNHPELVRRL GIIGINTALE
FDIYGNVNST HVCGTKMMNG IGGSGDFARN AHLAIFVTKS IAKGGDISSV VPFASHIDHA
EHDVDILVTE QGLADLRGLA PRERARAVID HCAHPMYRDA LNDYFDRACE KGGQTPHILR
EALSWHCNFE ETGHMLTTQD QAKKSA
//