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Database: UniProt
Entry: N1VL70_9LEPT
LinkDB: N1VL70_9LEPT
Original site: N1VL70_9LEPT 
ID   N1VL70_9LEPT            Unreviewed;       520 AA.
AC   N1VL70;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EMY60454.1};
DE            EC=2.8.3.- {ECO:0000313|EMBL:EMY60454.1};
GN   ORFNames=LEP1GSC203_2454 {ECO:0000313|EMBL:EMY60454.1};
OS   Leptospira terpstrae serovar Hualin str. LT 11-33 = ATCC 700639.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1257025 {ECO:0000313|EMBL:EMY60454.1, ECO:0000313|Proteomes:UP000012371};
RN   [1] {ECO:0000313|EMBL:EMY60454.1, ECO:0000313|Proteomes:UP000012371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT 11-33 {ECO:0000313|EMBL:EMY60454.1,
RC   ECO:0000313|Proteomes:UP000012371};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   Fouts D.E.;
RL   Submitted (MAR-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:EMY60454.1}.
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DR   EMBL; AOGW02000016; EMY60454.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1VL70; -.
DR   STRING; 1257025.LEP1GSC203_2454; -.
DR   Proteomes; UP000012371; 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:EMY60454.1}.
FT   DOMAIN          29..234
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          340..486
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        311
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         381
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         401
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         405
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         425
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   520 AA;  57792 MW;  4CC5C96B5B26B78C CRC64;
     MDFLFLGNLF IFGQRREFTL MAVTNALIEQ KIKSAEEVAA LLPRNVTLGC SGFTPAGYPK
     LIPVAFAKRI EDEKKLGNEF SINLYAGAST GEELDGALAK TGALKLRIPY QSNSHLRNLI
     NQGETDFIDM HLSHVVKYIE HGILPKIDAA IVEAIEVTVD GKIYLSTSSG MSATYIQNAE
     SVYIELTDTH PLELKGYHDI YLPNHHEKGL PINILNPGDR IGLPYIQVSP DKIKGIVRSN
     KPDAATVFKT PDEDCQNIAA HVLSFIQHEI KKGRIPKEYL PYQNGVGNIA NAVLASMAKD
     PNFHSIQMYT EVVQDSVFDL IDAGKLEIAS TSALTFSEKG LKRFHENISE WKSKFVIRPQ
     EISNHPEVIR RMGLIAMNTA IEVDIYGNVN STHVMGTSMM NGIGGSGDFT RNSHLCIFMT
     PSLAKEGNIS AVVPMVSHTD HNEHSTMIFV TEQGLADLRG CPPKKRAELI INNCAHPIYR
     DKLREYYENA LRVSKGKHTP HDLEKALSWH VQFLKTGSMK
//
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