GenomeNet

Database: UniProt
Entry: A0A1S9AGM4_9BURK
LinkDB: A0A1S9AGM4_9BURK
Original site: A0A1S9AGM4_9BURK 
ID   A0A1S9AGM4_9BURK        Unreviewed;       559 AA.
AC   A0A1S9AGM4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=AMP-dependent synthetase {ECO:0000313|EMBL:OON62442.1};
GN   ORFNames=B0920_02975 {ECO:0000313|EMBL:OON62442.1};
OS   Massilia sp. KIM.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1955422 {ECO:0000313|EMBL:OON62442.1, ECO:0000313|Proteomes:UP000190838};
RN   [1] {ECO:0000313|EMBL:OON62442.1, ECO:0000313|Proteomes:UP000190838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM {ECO:0000313|EMBL:OON62442.1,
RC   ECO:0000313|Proteomes:UP000190838};
RA   Vikram S., Kabwe M.H., Bezuidt O., Govender N., Makhalanyane T.P.;
RT   "Genome sequence of Massilia sp. KIM isolated from grassland biome soil in
RT   South Africa.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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:OON62442.1}.
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; MVAD01000001; OON62442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9AGM4; -.
DR   STRING; 1955422.B0920_02975; -.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000190838; Unassembled WGS sequence.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190838}.
FT   DOMAIN          45..389
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          452..529
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          539..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  62796 MW;  BBB20195EC33CCDF CRC64;
     MTPTQRFLQA RDFLQQHRTD YETAYRGYQR PRFENFNWAL DFFDHQARDN HAPALWVVDE
     DGSEQKISFA DMAARSSQVA EWLRQAGVER GDRVLLMLPN RVELWEIMLA GIKLGAVLVP
     TTMLVSGADL ADRLERGRIK HVIAQASEAH KFEALPGNYT RIAVGGALEG WRDFDDCRST
     LAVFTPEGET RATDPLLLYF TSGTTAKPKL VLHSHQSYPV GHLSTMYWIG LQRGDVHWNI
     SSPGWAKHAW SCFFAPWNAG ATVFVYNYER FSARAALDTI VRCGVTSLCA PPTVWRMMIK
     EDLAAWKPPL RELVGAGEPL NPEVIEQVER AWGIRIRDGF GQSESTCQIG NSPGQPIKPG
     SMGRPLPGYE VALLDIDDQP APEGEIAVKL DAEPIGLMLC YEGDEAKTAE VMRGGYYHTG
     DTASRDADGY YFYVGRNDDV FKSSDYRISP FELESVLIEH ESVLEAAIVP SPDPLRLSVP
     KAFVTLRQGR EPSREAAAAL FAFTRERLAP YKRIRRIEFR ELPKTISGKI RRVELRKEEA
     ARGEAAPAGL EYREEDFPA
//
DBGET integrated database retrieval system