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Database: UniProt
Entry: J2LK01_9BURK
LinkDB: J2LK01_9BURK
Original site: J2LK01_9BURK 
ID   J2LK01_9BURK            Unreviewed;       636 AA.
AC   J2LK01;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Propionate--CoA ligase {ECO:0000313|EMBL:EJL85543.1};
GN   ORFNames=PMI15_01788 {ECO:0000313|EMBL:EJL85543.1};
OS   Polaromonas sp. CF318.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL85543.1, ECO:0000313|Proteomes:UP000007275};
RN   [1] {ECO:0000313|EMBL:EJL85543.1, ECO:0000313|Proteomes:UP000007275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF318 {ECO:0000313|EMBL:EJL85543.1,
RC   ECO:0000313|Proteomes:UP000007275};
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:EJL85543.1}.
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DR   EMBL; AKIV01000051; EJL85543.1; -; Genomic_DNA.
DR   RefSeq; WP_007866896.1; NZ_AKIV01000051.1.
DR   AlphaFoldDB; J2LK01; -.
DR   PATRIC; fig|1144318.3.peg.1731; -.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000007275; Unassembled WGS sequence.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR032387; ACAS_N.
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   InterPro; IPR012694; Propion_PrpE.
DR   NCBIfam; TIGR02316; propion_prpE; 1.
DR   PANTHER; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 1.
DR   Pfam; PF16177; ACAS_N; 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:0000313|EMBL:EJL85543.1}.
FT   DOMAIN          4..58
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          60..453
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          517..600
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   636 AA;  69790 MW;  278587F888512A11 CRC64;
     MTSYTDFYRQ SIDQPEAFWT EQAKLIDWHK PFTRVCNDDK PPFVQWFEGG QINLCHNAVD
     RHLKDRPDQA ALIYVSSETG VEKTYSFKEL HAEVQRMAAS LLAMGVVKGD RVLIYMPMIP
     EAAFAMLACA RIGAIHCVVF GGFASGSLAS RIDDATPRVI ISADAGSRGG KVVAYKPLLD
     EAIRLAGHQP EAVLLVNRGL APMNIVAGRD LHWETLRAKY MHAQVHCEWL DSSAISYTIY
     TSGTTGKPKG VQRDTGGYAV ALAASMKHIF DGRAGETYFS TSDIGWVVGH SYIVYGPLIA
     GMATIMYEGL PTQGMDGQPN AAIWWRLVEK YKVTGMFSAP TAVRVLKKQD PGLLKKHDLS
     SLRAFYLAGE PLDEPTARWI SEGLNVPIID NYWQTESGWP IITLANAVEK KPSRFGSPGV
     PMYGYKVKIL HESTGEELTQ PNEKGVVVIE GPTPPGFMQT IWKDDARFVN TYWKSVPGKM
     VYSTFDWGIR DEDGYFFILG RTDDVINVAG HRLGTREIEE SISGHAGVAE VAVIGVADPL
     KGQVAMAFAV PKDSSVLMDT AAAMKLEGEI MKRVDGDLGA VARPARVHFV SALPKTRSGK
     MLRRAIQAVC EGRDAGDLTT MDDPAALQQI RDRVAG
//
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