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Database: UniProt/TrEMBL
Entry: E3EJF7_PAEPS
LinkDB: E3EJF7_PAEPS
Original site: E3EJF7_PAEPS 
ID   E3EJF7_PAEPS            Unreviewed;       529 AA.
AC   E3EJF7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Acyl--CoA ligase {ECO:0000313|EMBL:ADO56507.1};
GN   Name=acsA1 {ECO:0000313|EMBL:ADO56507.1};
GN   ORFNames=PPSC2_11910 {ECO:0000313|EMBL:ADO56507.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO56507.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO56507.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO56507.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP002213; ADO56507.1; -; Genomic_DNA.
DR   RefSeq; WP_013371112.1; NC_014622.2.
DR   AlphaFoldDB; E3EJF7; -.
DR   STRING; 1406.LK13_24230; -.
DR   KEGG; ppm:PPSC2_11910; -.
DR   PATRIC; fig|886882.15.peg.2523; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_9; -.
DR   OrthoDB; 9757771at2; -.
DR   Proteomes; UP000006868; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   CDD; cd05972; MACS_like; 1.
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; 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.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADO56507.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   DOMAIN          24..386
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          436..514
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   529 AA;  59100 MW;  D53398FF7A33164E CRC64;
     MTDQQQWLAP EYYNMTSEME HHEAGKTALK WLSETGEYEE ITYGELLKKA NRLAGGLASL
     GFNKGDRVLV VVPRRIIAYV IYLACLKLGL AVIPSSEMLR AKDIAYRLRH SEARAVIAWT
     DVTSEVDKIS DDLPALDYRI VVPGDRTVGA QGWLVLDELM EGQEDIFEAV KTHRDDMAIL
     AYTSGTTGNP KGVVHSHGWG YAHLRITSPW LDIRASDIVW ATAAPGWQKW IWSPFLSVLG
     NGATGFVYNG PFRPGRYLQL LQQYGVQVLC CTPTEYRIMA KTAGLDQYDL SRLRSAVSAG
     EPLNQEVINK FQEQFNITIR DGYGQTESTL IIGNLRDVPL RTGSMGKSIA PGLVEVVDED
     GIPLAPGQVG DIAVRADLPA LFHTYYHDPE RKLASVHGDY FVTGDRARKD EDGYFWFEGR
     GDDIIISSGY TIGPFEVEEA LMKHDSVQEC AAVASPDEVR GHVVKAYIVL KAGIEGSPEL
     VKELQHHVKT WTAPYKYPRK IEFIEELPKT SSGKIRRVEL RELEKQSVL
//
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