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Database: UniProt
Entry: A0A0M2R772_9PROT
LinkDB: A0A0M2R772_9PROT
Original site: A0A0M2R772_9PROT 
ID   A0A0M2R772_9PROT        Unreviewed;       632 AA.
AC   A0A0M2R772;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:KKJ76264.1};
DE            EC=6.2.1.17 {ECO:0000313|EMBL:KKJ76264.1};
GN   Name=prpE {ECO:0000313|EMBL:KKJ76264.1};
GN   ORFNames=WH95_13660 {ECO:0000313|EMBL:KKJ76264.1};
OS   Kiloniella litopenaei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Kiloniellaceae; Kiloniella.
OX   NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ76264.1, ECO:0000313|Proteomes:UP000034491};
RN   [1] {ECO:0000313|EMBL:KKJ76264.1, ECO:0000313|Proteomes:UP000034491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-1 {ECO:0000313|EMBL:KKJ76264.1,
RC   ECO:0000313|Proteomes:UP000034491};
RA   Shao Z., Wang L., Li X.;
RT   "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT   of Pacific white shrimp, Penaeus vannamei.";
RL   Submitted (MAR-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:KKJ76264.1}.
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DR   EMBL; LANI01000020; KKJ76264.1; -; Genomic_DNA.
DR   RefSeq; WP_046508218.1; NZ_LANI01000020.1.
DR   AlphaFoldDB; A0A0M2R772; -.
DR   STRING; 1549748.WH95_13660; -.
DR   PATRIC; fig|1549748.8.peg.1464; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000034491; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Ligase {ECO:0000313|EMBL:KKJ76264.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034491}.
FT   DOMAIN          6..58
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          61..447
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          512..590
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   632 AA;  68996 MW;  1DB40D424DCB464C CRC64;
     MGLFDDVQAR SLAKPEIFWA EAASEIDWYK PYTKVLDGSD APFYRWFSGG ELNTCYNALD
     RHVEQGRGEQ TALIYDSPVT DTKENITYSD LLKRVAKFAG SLAQLGVAKG DRVIIYMPMI
     PEAAVAMLAC ARLGAVHSVV FGGFAANELA TRIDDCSPKV IVSASCGIEV SKVIPYKPLL
     DEAIDLSTHK PDHCVIWQRP QIEASMTAER DVDWAEIEGQ ASAVDCVPVA ATDPLYILYT
     SGTTGQPKGI VRDNGGHAVA LHWSMKNIYN VEPGEVFWGA SDVGWVVGHS YIVYGPLIYG
     ATSVMYEGKP VGTPDPGAFW RVISEHNVSV LFTAPTAFRA IRQQDPDASY LDKYDLSCFR
     TLFLAGERCD PDTLNWALDK LKVPVIDHWW QTETGWPIAS NCLGIEELPI VAGSPARSVP
     GWDVRILDAD DHSEMPAGDI GAIVCKLPLP PGTFSTLWNA KERHRQAYLT GFPGYYETGD
     AGYKDENGYI YVMSRTDDII NVAGHRLSTG AMEEVLAAHE DVAECAVIGV ADKLKGQLPL
     GFMVLKAGAQ KSHSDVVAEV VQKVRHDIGP VAAFKLAVVV GRLPKTRSGK ILRATMRKIA
     DSEDFKVPAT IDDPVILDEI RVALQSIGYG NT
//
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