ID   A0A1I1IVK7_9BURK        Unreviewed;       638 AA.
AC   A0A1I1IVK7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:SFC40286.1};
GN   ORFNames=SAMN05216344_11655 {ECO:0000313|EMBL:SFC40286.1};
OS   Polaromonas sp. OV174.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1855300 {ECO:0000313|EMBL:SFC40286.1, ECO:0000313|Proteomes:UP000218980};
RN   [1] {ECO:0000313|EMBL:SFC40286.1, ECO:0000313|Proteomes:UP000218980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV174 {ECO:0000313|EMBL:SFC40286.1,
RC   ECO:0000313|Proteomes:UP000218980};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; FOKZ01000016; SFC40286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1IVK7; -.
DR   STRING; 1855300.SAMN05216344_11655; -.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000218980; Unassembled WGS sequence.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000218980}.
FT   DOMAIN          8..62
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          65..456
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          521..604
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   638 AA;  69786 MW;  E1EF8D620DFA7E4D CRC64;
     MQNTLTNYSD FYRQSVEQPD AFWAEQAQLI DWHQPFSRVC NDDNPPFVRW FEGGKTNLCH
     NAVDRHLAAR AEQAALICVS SETGQEKIYS FKALHQEVQR MAASLQALGV QQGDRVLIYM
     PMMAEAAFAM LACARLGAIH CVVFGGFASG SLASRIEDAT PKVIVSADGG SRGGKALAYK
     PLLDEAIRLS SHKPQALLLA DRGLAPMALV AGRDHLWSDL REQHLDAQVA CAWLDAAAVS
     YTIYTSGTTG KPKGVQRDTG GYAVALAASL KHIFDGRAGE TFFSTSDIGW VVGHSYIVYG
     PLIAGMSSIM YEGLPTQGMD GKPNGGIWWQ LVEKYRVTVM FSAPTAVRVL KKQDPALLTK
     YDLSSLRALF LAGEPLDEPT ARWISEGLKV PIIDNYWQTE SGWPILTIAN GVEKKPSKFG
     SPGVPMYGYK VKLMHETSGE ELTQPGEKGV LVIESPTPPG FMQTVWQDDA RFINTYWKSI
     AGKTVYNTFD WGIRDADGYY FILGRTDDVI NVAGHRLGTR EIEESISGHA QVAEVAVVGV
     ADALKGQVAM AFVVLKDASL MADEAASLKL EGEIMKRVDG DLGALARPAR VRFVSALPKT
     RSGKLLRRAI QAVCEDRDTG DLTSMEDPAV LQQIRERM
//