ID A0A1W6ZEW4_9BORD Unreviewed; 629 AA.
AC A0A1W6ZEW4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Propionate--CoA ligase {ECO:0000313|EMBL:ARP95859.1};
GN ORFNames=CAL15_16630 {ECO:0000313|EMBL:ARP95859.1};
OS Bordetella genomosp. 13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463040 {ECO:0000313|EMBL:ARP95859.1, ECO:0000313|Proteomes:UP000194161};
RN [1] {ECO:0000313|EMBL:ARP95859.1, ECO:0000313|Proteomes:UP000194161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU7206 {ECO:0000313|EMBL:ARP95859.1,
RC ECO:0000313|Proteomes:UP000194161};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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; CP021111; ARP95859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6ZEW4; -.
DR STRING; 463040.CAL15_16630; -.
DR KEGG; bgm:CAL15_16630; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000194161; Chromosome.
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; 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:ARP95859.1}.
FT DOMAIN 5..58
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 60..444
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 511..594
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 629 AA; 69536 MW; E490804ABC62DFB9 CRC64;
MEKTRDFHYR SIHDPDGFWR EQAQRIHWET PFSQVLDDER LPFARWFVGG RTNLCYNAVD
RWLPQYADRV ALAWVSTEVD QERLYTRQQL YAEVNAVAAM LREQGVGPGD RVLIYMPMVP
EAVFAMLACA RIGAVHSVVF GGFASVNLAQ RIDDAAPKVL MCADGGSRAG KVVPYKPLVD
KALSLCGKPP RAVVVLDRGL VPFQPEPGRD LDYAELRRRH DGAQVPVEWV ESSEPSYVLY
TSGTTGRPKG VQRDTGGYAV ALAASMEYLF DGKPGDTFFC TSDIGWVVGH SYIVYGPLIG
GQTSVLYEGT PVRPDGAILW KLVERFGVNT LFSAPTAVRV LKRQDPELLR RHDLSTLRAV
YLAGEPLDEP TARWVSEGLG KPIIDNYWQT ESGWPILSAQ PGVERVATRF GSPSFPTYGF
DVRIVSEATG EDLEPGQKGV VAIEPPLPPG AMSTIWGDDE RFVQTYFTSI PGRQVYSTFD
WGRVDEDGYW YILGRTDDVI NVAGHRLGTR EIEESINSHA GVAECAVVGV ADELKGQVAM
AFVVLKRPDA AQHADDARAL EGDIMRVVED QLGAVARPSR IRFVGALPKT RSGKVLRRAI
VAVCENRDPG DLTTIEDPTA LQQIKESLQ
//
