ID A0A0S8CTA2_9PROT Unreviewed; 632 AA.
AC A0A0S8CTA2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Propionate--CoA ligase {ECO:0000313|EMBL:KPK27257.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:KPK27257.1};
GN Name=prpE {ECO:0000313|EMBL:KPK27257.1};
GN ORFNames=AMJ66_11305 {ECO:0000313|EMBL:KPK27257.1};
OS Betaproteobacteria bacterium SG8_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK27257.1, ECO:0000313|Proteomes:UP000051602};
RN [1] {ECO:0000313|EMBL:KPK27257.1, ECO:0000313|Proteomes:UP000051602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK27257.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK27257.1}.
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DR EMBL; LJTS01000228; KPK27257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CTA2; -.
DR PATRIC; fig|1703389.3.peg.1332; -.
DR Proteomes; UP000051602; 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:KPK27257.1}.
FT DOMAIN 5..59
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 62..444
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 513..596
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 632 AA; 69693 MW; FD5F70AE813B7AF0 CRC64;
MGQKYQQFYR RSIEDRDAFW TEQAALIDWN KPFDQVLEYS NPPFARWFVG GQTNLCHNAI
DRHLDARGGQ PALIYISTET GAEKTYSYDE LHEEVVRCAA VLRGLGVGKG DVVLIYMPMI
PEAIFAMLAS VRLGAVHSVV FGGFAPASLA LRIDDAKPKV MITSDAGMRA GRVIAYKHLV
DEAMRLSQSP PEKVVIVNRG LDSNMAITEG RDLDYATLAR QHAGEDVPVT WLESSDPSYV
MYTSGTTGKP KGVQRDTGGY AVALAASMKH IYCGNAGDTM FTTSDIGWVV GHSYIVYAPL
ICGLTTIVYE GVPIRPDPGI WWKIVQDYKV KVMFSSPTGV RVLKKQDPEY MSKYDMSSLK
HIFLAGEPLD EPTHTWLTEA LGKPVIDHYW QTETGWPILT SVPGVEETPI KFGSPSFPAY
GYDLKLLRES DASEADADEK GVVAIIPPLP PGCMTTLWGD DERFVNTYFS TFTSKLVYST
FDWGIRDRDG YYFILGRTDD VINVAGHRLG TREIEEAVQA HPNIAEVAVV GVDDQLKGQM
PLAFAVVKDA SRIATAELKA AEEKAVMAKV DAQLGAIARP RRVYFVSTLP KTRSGKMLRR
SIQALAEGRD PGDLTSLEDP GALEQIQQAV KG
//
