ID A0A0R0C422_9GAMM Unreviewed; 626 AA.
AC A0A0R0C422;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:KRG64525.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:KRG64525.1};
GN Name=prpE {ECO:0000313|EMBL:KRG64525.1};
GN ORFNames=ABB26_07870 {ECO:0000313|EMBL:KRG64525.1};
OS Stenotrophomonas humi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG64525.1, ECO:0000313|Proteomes:UP000050864};
RN [1] {ECO:0000313|EMBL:KRG64525.1, ECO:0000313|Proteomes:UP000050864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG64525.1,
RC ECO:0000313|Proteomes:UP000050864};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG64525.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDJI01000013; KRG64525.1; -; Genomic_DNA.
DR RefSeq; WP_057633122.1; NZ_LDJI01000013.1.
DR AlphaFoldDB; A0A0R0C422; -.
DR STRING; 405444.ABB26_07870; -.
DR PATRIC; fig|405444.3.peg.581; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000050864; Unassembled WGS sequence.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
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; IPR020845; AMP-binding_CS.
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.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KRG64525.1}.
FT DOMAIN 3..57
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 60..446
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 510..590
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 626 AA; 68980 MW; D0FC517464850140 CRC64;
MQYEQIYRRS IEAPEEFWAE EAKAIHWHRP PQQILDYSNP PFRRWFVGGE TNLCYNAVDR
HLAERAEQLA LVAISTETNV TREITYRELY REVNAFAAML KQLDVGRGDR VVIYMPNMPE
AVFAMLACAR IGAVHSVVFG GFAAHNLALR IDDAQPKLLI AADAGMRGGK VIPYKAMVDA
ACAEAQSPPP KVLIVSRGLD AAEPKVAGRD EDYAALRAQV GDVEVPVEWL ESNEPSYLLY
TSGTTGKPKG VQRDVGGYAV AMAQSIRTVF DCAPGQVMFS TSDVGWAVGH SYNVYGPLIG
GCTSLLYEGL PINPDAGIWW ALCEQYGVRT MFSSPTAIRV LKKHDVDFID RHDLSELKYL
FLAGEPLDQP TAQWISGALH KPVIDNYWQT ETGWPALTLL PGLDMKPVKF GSPGFPNLGY
RMKVIDEQSG EEVAPGQKGV LVIQPPLPPG CMSTVWNDDE RFLKSYFSHF NELLYSSLDW
AIRDEEGYTF ILGRTDDVIN VAGHRLGTRE IEEAISSHPR VAEAAVIGVH DELKGQVPLV
FVTLKQAAAA EETATLAAEM MQRVTSSLGA VARPAHVHIV NALPKTRSGK LLRRSLQALA
EQRDPGDLST LDDPGALDEI RRALGK
//
