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Database: UniProt
Entry: Q1J402_SPHAL
LinkDB: Q1J402_SPHAL
Original site: Q1J402_SPHAL 
ID   Q1J402_SPHAL            Unreviewed;       495 AA.
AC   Q1J402;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:ABF54921.1};
GN   OrderedLocusNames=Sala_3218 {ECO:0000313|EMBL:ABF54921.1};
OS   Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS   (Sphingomonas alaskensis).
OG   Plasmid F {ECO:0000313|Proteomes:UP000006578}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF54921.1, ECO:0000313|Proteomes:UP000006578};
RN   [1] {ECO:0000313|EMBL:ABF54921.1, ECO:0000313|Proteomes:UP000006578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13593 / LMG 18877 / RB2256
RC   {ECO:0000313|Proteomes:UP000006578};
RC   PLASMID=Plasmid F {ECO:0000313|Proteomes:UP000006578};
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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DR   EMBL; CP000357; ABF54921.1; -; Genomic_DNA.
DR   RefSeq; WP_011536545.1; NC_008036.1.
DR   AlphaFoldDB; Q1J402; -.
DR   KEGG; sal:Sala_3218; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_5; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000006578; Plasmid F.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:ABF54921.1};
KW   Plasmid {ECO:0000313|EMBL:ABF54921.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006578}.
FT   DOMAIN          12..339
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          399..474
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   495 AA;  53869 MW;  E99B8E07AEC642D1 CRC64;
     MEVRRISDAL KVRAQHQADE IAHDDTRRQI SFAEWDREVD EVAGGLAAAG LVPGDRVFLP
     ISNFHAVEMA IAVFAVFRAG GIACPINTRL NPKEIAEYAA LCEPRFCITD APDRVRDLKL
     AACWHAEDMP RNLTALPDQA SLDPGADAEI LATSGTTGKI KGVVISHPDL MTGVTGYNMD
     RSRSTLNALP LTGSGGNIGI VMLPARGGAT AITQPKFDPK GFLDLVREKR PNLVYLVPSM
     LRLVLDHPDA PDYDFSGVKY LMTGTAPLPH DSVKRAMDLW PHLRIRNSYG MSEGGVGVST
     TSAEQVLKPG CVGKLPKHMQ LRDEAGNVIT TVGVVGEIYG WQKHPRRYWN DEQATADSFR
     GGWTKTGDLG FIDEDGDLIM AGRSKELIIR GGYNITPLEI ETVLHLHPAV QQAAVVGIPH
     EILGEDIAAA VTLRPGKTAE TEEILSFCRE HLADNKVPRT LVIMDSLPLN PNGKILKKYL
     AEPLARAAEA RRRAA
//
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