ID A0A0A1FFB6_9BURK Unreviewed; 630 AA.
AC A0A0A1FFB6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Propionate--CoA ligase {ECO:0000313|EMBL:AIY43206.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:AIY43206.1};
GN ORFNames=LT85_4048 {ECO:0000313|EMBL:AIY43206.1};
OS Collimonas arenae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY43206.1, ECO:0000313|Proteomes:UP000030302};
RN [1] {ECO:0000313|EMBL:AIY43206.1, ECO:0000313|Proteomes:UP000030302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cal35 {ECO:0000313|EMBL:AIY43206.1,
RC ECO:0000313|Proteomes:UP000030302};
RA Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT "Structure and function of bacterial communities in ageing soils: insights
RT from the Mendocino ecological staircase.";
RL Soil Biol. Biochem. 69:265-274(2014).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CP009962; AIY43206.1; -; Genomic_DNA.
DR RefSeq; WP_038492465.1; NZ_CP009962.1.
DR AlphaFoldDB; A0A0A1FFB6; -.
DR STRING; 279058.LT85_4048; -.
DR KEGG; care:LT85_4048; -.
DR HOGENOM; CLU_000022_3_6_4; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000030302; 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; 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:AIY43206.1}.
FT DOMAIN 5..57
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 59..443
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 513..594
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 630 AA; 69229 MW; 84701C29E8B6A52D CRC64;
MSFASFYQRS IDEPSTFWAE QARRIDWHHP FSQVLDDSRP PFARWFVDGT TNLCHNAVDR
WVATRGDQPA LIAISTETDT EKTYTFRELH AEVNRTAAIM QSLGVGRGDR VLIYMPMIAE
ATFAMLACAR IGAIHSVVFG GFASNSLASR IDDATPKLIV SADAGSRGGK VVAYKGLLDD
AIKLAQHKPA HVLMVNRGLA AMETMAGRDV DYTEQRRLHI DAKVPVVWLE SNEVSYILYT
SGTTGKPKGV QRDVGGYAVA LATSMDTIFC SKGGGTFFCT SDIGWVVGHS YIVYGPLIAG
MATILYEGLP IRPDGGVWWS IVEKYKVTRM FSAPTAIRVL KKQPPELMQK YNLSSLQALY
LAGEPLDETT SRWISEALGV PIIDNYWQTE SGWPIMTIAK NIENKPSKLG SPGVPMYGYK
VQLLNEATGE LCGANEKGVV VIEWPLPPGC MQTIYGDDQR CVDTYWATPI PQTGRPAYST
FDWGIRDEDG YYFILGRTDD VINVAGHRLG TREIEESISS HPNVSEVAVV GVEDKLKGQV
AVAFVIPKVA ESTAEGRAAL EEEIMRVVDK QIGSVGRPAH VYVVNLLPKT RSGKLLRRSI
QAICEGRDPG DLTTIEDPAS LQQIKDALRG
//
