ID A0A0Q9KTJ8_9MICO Unreviewed; 639 AA.
AC A0A0Q9KTJ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Propionate--CoA ligase {ECO:0000313|EMBL:KRE43083.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:KRE43083.1};
GN Name=prpE {ECO:0000313|EMBL:KRE43083.1};
GN Synonyms=yahU {ECO:0000313|EMBL:KRE43083.1};
GN ORFNames=ASG74_08775 {ECO:0000313|EMBL:KRE43083.1};
OS Knoellia sp. Soil729.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE43083.1, ECO:0000313|Proteomes:UP000051965};
RN [1] {ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE43083.1, ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|EMBL:KRE43083.1,
RC ECO:0000313|Proteomes:UP000051965};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE43083.1}.
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DR EMBL; LMSA01000002; KRE43083.1; -; Genomic_DNA.
DR RefSeq; WP_056143387.1; NZ_LMSA01000002.1.
DR AlphaFoldDB; A0A0Q9KTJ8; -.
DR STRING; 1736394.ASG74_08775; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000051965; Unassembled WGS sequence.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR CDD; cd05967; PrpE; 1.
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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
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.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KRE43083.1}.
FT DOMAIN 6..60
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 69..452
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 517..598
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 639 AA; 68499 MW; F00A109EFC3BBBF1 CRC64;
MSTDGYAAAY GQSLDDPDTF WRDAAEQIEW ITAPMTVLDS SNAPLHRWFP GATLNTCFNA
LDRHVRDGRG EQPALIHDSP VTATKETITY ADLLARVATF AGALASLGVE KGDRVVIYMP
MVPEAVVAML ACARLGAIHS VVFGGFAPTE LAARIEDAQP KVVVAASCGI EPSRVVEYKP
MLDAALDRSS HKPESVIVFQ REQARAAVGE RDTDWEELDW ADVVADAEPA DCVEVEATDP
LYILYTSGTT GRPKGIVRDN GGHAVALRWS MDNIYGINAG DVWFTASDVG WVVGHSYIVY
APLLTGATTV LYEGKPVGTP DAGAFWRVIV EHKVRAMFTA PTAYRAIKRD DPRGELLAQH
DLSSLETVFL AGERLDPDTY EWAASTLGVP VVDNWWQTET GWPIAANPRG LEPMPIKAGS
PTVAMPGYAV SILDETGAPL PAGEEGAIAI RLPLPPGTLV TLWGDDQRYI DGYLSTYPGY
YATGDGGYVD EDGYLFVMGR TDDVLNVAGH RLSTGSIEAA LAGHPDVAEC AVIGVADELK
GQLPRGLVVL KGGIDGSGAE GERIRKELVQ RVRDEVGAVA ALRQVDIVAG LPKTRSGKIL
RKTMREIADG RTPTIPGTIE DASVLDTLTP VLRPQAATS
//
