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Database: UniProt
Entry: J3DH78_9BURK
LinkDB: J3DH78_9BURK
Original site: J3DH78_9BURK 
ID   J3DH78_9BURK            Unreviewed;       549 AA.
AC   J3DH78;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Acyl-CoA synthetase/AMP-acid ligase {ECO:0000313|EMBL:EJL91909.1};
GN   ORFNames=PMI16_01398 {ECO:0000313|EMBL:EJL91909.1};
OS   Herbaspirillum sp. CF444.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL91909.1, ECO:0000313|Proteomes:UP000007296};
RN   [1] {ECO:0000313|EMBL:EJL91909.1, ECO:0000313|Proteomes:UP000007296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF444 {ECO:0000313|EMBL:EJL91909.1,
RC   ECO:0000313|Proteomes:UP000007296};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL91909.1}.
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DR   EMBL; AKJW01000026; EJL91909.1; -; Genomic_DNA.
DR   RefSeq; WP_007877781.1; NZ_AKJW01000026.1.
DR   AlphaFoldDB; J3DH78; -.
DR   STRING; 1144319.PMI16_01398; -.
DR   PATRIC; fig|1144319.3.peg.1414; -.
DR   eggNOG; COG0365; Bacteria.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000007296; 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   CDD; cd05971; MACS_like_3; 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   InterPro; IPR049515; MACS_put.
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:EJL91909.1}.
FT   DOMAIN          32..401
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          451..529
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   549 AA;  60329 MW;  D7C8689CA0723A88 CRC64;
     MLPIEARPYQ EINDAFRWNI PEYYNIGVDV CDKWAETDPG RLALIHVAAD GSSRRYSFGE
     IKESSDRLAN LFLASGANTG DRIGILLPQA PETAMAHVAA YKIGAIAIPL FALFGAEALE
     YRLHNSGTRV VVTNAAGAAK LAGIRDRLPA LQTILTIDGA FHGTMDLHQA LKQASSDLTP
     VKTKADDPAV IIYTSGTTGQ PKGALHAHRV LLGHLPGVEL SHNLFPLEGD LLWTPADWAW
     IGGLLDVFLP AWHHGVPLVA HRFEKFTGEA AFQLLQDYGV RNTFLPPTAL KMMRTVAEPE
     KRWRYQLRSV ASGGESLGME LLDWGRQTFG LTINEFYGQT ECNMTVSSCA AIMDCKPGAI
     GRAAIGHKLA IVDAQGRVLP PGSDGNIAVQ RPDPVMFLQY WNNPQATQDK FVGDWLLTGD
     TGCMDEDGYI RFVGRDDDVI TSAGYRIGPG EIEDNILQHP AVKMVAVIGS PDAQRTEIVV
     AVIVLKDGVT GDDELKREIQ EHVKVRLAAH EYPREIFFVD ELPMTTTGKV IRRELRARVS
     EWRTQPQQA
//
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