ID K0I1B6_9BURK Unreviewed; 633 AA.
AC K0I1B6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:AFU46030.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:AFU46030.1};
GN Name=prpE {ECO:0000313|EMBL:AFU46030.1};
GN ORFNames=C380_11645 {ECO:0000313|EMBL:AFU46030.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU46030.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU46030.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU46030.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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; CP003872; AFU46030.1; -; Genomic_DNA.
DR RefSeq; WP_015014046.1; NC_018708.1.
DR AlphaFoldDB; K0I1B6; -.
DR STRING; 358220.C380_11645; -.
DR KEGG; ack:C380_11645; -.
DR PATRIC; fig|358220.3.peg.2371; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_5_4; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000006306; Chromosome.
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; 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:AFU46030.1}.
FT DOMAIN 7..61
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 66..450
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 515..598
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 633 AA; 69291 MW; 1E496068D2469D41 CRC64;
MTAHSTYADF YRQSIDHRDT FWSEQAKLID WKTPPQQVCD YSNPPFAKWF VGGTTNLCHN
AVDRHLATRA SQAALVAIST ETDTERSYSF AELHAEVQRM AAVLLSLGVK KGDRVLIYMP
MIAEAAFAML ACVRIGALHS VVFGGFASGS LASRIEDAEP VAVVSADAGS RGGKVVPYKP
LLDEAIALSK HKPTAVLMVN RGLAPMHLQA GRDHEWAPLR EQHLHTVVAC EWVESTHPSY
TLYTSGTTGK PKGVQRDTGG YTVALAASMK HIFDAKPGET YFATSDIGWV VGHSYIIYGP
LIAGMTTIMY EGLPTRPDAG VWWSIVEKYR VTHMFSAPTA VRVLKKQDPA YLAKYNVKSL
KALWLAGEPL DEPTAQWISD ALSVPIIDNY WQTETGWPIL TLANGVEPQT ARFGSPGKAM
YGYDVKLIDE ATGQELTGPN QKGVVAIEGP LPPGCMQTVW RDDARFVNTY WKSIPGRLIY
STFDWGIRDA DGYHFILGRT DDVINVAGHR LGTREIEESI ASHPNIAEVA VVGVADSLKG
QVAMAFAVVR DASGLTDDAA RLKLEGEVMK QVDHQLGAVA RPSRVYFVTV LPKTRSGKLL
RRALQAVAER RDPGDLTTME DPAALQQVKD LVG
//
