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Database: UniProt
Entry: A0A0J1EXM2_9MICC
LinkDB: A0A0J1EXM2_9MICC
Original site: A0A0J1EXM2_9MICC 
ID   A0A0J1EXM2_9MICC        Unreviewed;       650 AA.
AC   A0A0J1EXM2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:KLU10169.1};
DE            EC=6.2.1.17 {ECO:0000313|EMBL:KLU10169.1};
GN   Name=prpE {ECO:0000313|EMBL:KLU10169.1};
GN   ORFNames=ABL57_08170 {ECO:0000313|EMBL:KLU10169.1};
OS   Kocuria sp. SM24M-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU10169.1, ECO:0000313|Proteomes:UP000036489};
RN   [1] {ECO:0000313|EMBL:KLU10169.1, ECO:0000313|Proteomes:UP000036489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU10169.1,
RC   ECO:0000313|Proteomes:UP000036489};
RA   Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA   Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA   Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA   Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT   "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
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:KLU10169.1}.
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DR   EMBL; LDNX01000067; KLU10169.1; -; Genomic_DNA.
DR   RefSeq; WP_047802971.1; NZ_LDNX01000067.1.
DR   AlphaFoldDB; A0A0J1EXM2; -.
DR   PATRIC; fig|1660349.3.peg.3727; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000036489; Unassembled WGS sequence.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
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:KLU10169.1}.
FT   DOMAIN          13..67
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          74..466
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          532..610
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   650 AA;  70606 MW;  FDD37E4559AB580A CRC64;
     MSTEQQTTQA EDYAEVYRRS VRDPERFWLE AARAVDWTRE PTVALDAAMA PLYRWFPDGE
     LNTSYNALDR HVEAGHGERT ALVYDSALLG VQERYSYARL RDEVALFAGA LAARGVGRGD
     RVLVYLPMIP QAAVAMLACA RLGAVHSVVF GGFAPKELAA RIDDSRPRVV VTTTGGLEPR
     RRIEYIPAIE EALRLARHEP GTVVVHERPG FETTVEQARE RAGHGEQPAV EWLGWDAAVE
     GAEPAAPVPV AATDPLYVLY TSGTTGAPKG VVRDNGGHAV AMTWSMRHIY DVGPGEVMWT
     ASDVGWVVGH SYIVYGPLLA GATTVLYEGK PVGTPDAGAF WRRVEDHGVK VLFTAPTALR
     AIRRADPEGE LVRRHDIGSL QALFVAGERL DPETYGWASR VLGVPVVDHW WQTETGWAIC
     ANPFGIERLP LKPGSPSVPV PGYRVEVLDP LGQPVATGEE GNIALRLPLP PGTLTTLWGD
     DRRFVDSYLT AFPGYYATGD SGHVDEDGYV YVMGRTDDVI NVSGHRLSTG AMEQVLASHP
     AVAECAVIGV ADPLKGQRPA GYVVLKSGVE VPEERLRDEL VALVRRQIGA VADFKDVAVV
     EGLPKTRSGK ILRKTMRQIA DGEDYTVPST IEDSTVLEAL EGVLRPPRAG
//
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