ID A0A0Q8QTZ4_9BURK Unreviewed; 630 AA.
AC A0A0Q8QTZ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Propionate--CoA ligase {ECO:0000313|EMBL:KRB89046.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:KRB89046.1};
GN Name=prpE {ECO:0000313|EMBL:KRB89046.1};
GN Synonyms=yahU {ECO:0000313|EMBL:KRB89046.1};
GN ORFNames=ASE07_02640 {ECO:0000313|EMBL:KRB89046.1};
OS Noviherbaspirillum sp. Root189.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB89046.1, ECO:0000313|Proteomes:UP000051303};
RN [1] {ECO:0000313|EMBL:KRB89046.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB89046.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB89046.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB89046.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRB89046.1}.
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DR EMBL; LMHZ01000012; KRB89046.1; -; Genomic_DNA.
DR RefSeq; WP_057290433.1; NZ_LMHZ01000012.1.
DR AlphaFoldDB; A0A0Q8QTZ4; -.
DR STRING; 1736487.ASE07_02640; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000051303; 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:KRB89046.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051303}.
FT DOMAIN 5..57
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 59..445
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 509..592
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 630 AA; 69201 MW; 452E3A7FB8B2332E CRC64;
MNFPDFYQQS ITDPQAFWDR EAKRIDWNEP YTQVLDYANP PFTKWFVGGK TNLCHNAVDR
WVAMQADKPA LIAISTETGT EKVYSFKELQ TEVMRAAAMM QSLGVGKGDR VLIYMPMVAE
AVFAMLACAR IGAIHSVVFG GFASNSLATR IDDAKPTLIV SADAGSRAGK AVAYKPLLDE
AIHHAQHKPA HVLMVNRGLV PTTMVAGRDV DYAELREQHF HAQVPVTWLE SNETSYILYT
SGTTGKPKGV QRDVGGYAVA LAASMKHIFC GNPGETYFST SDIGWVVGHS YIVYGPLIAG
MATVLYEGLP IRPDAGIWWS IVEKYKVTRM FSAPTAVRVL KKQPPEFMKK YDLSSLKALY
LAGEPLDETT SEWIASELGV PIIDNYWQTE TGWPILTVAC GVENKATRLG SPGVPMYGYK
VKLINESTGV ECGPNEKGVV VIEGPLPPGC MQTVYGDDER FVKTYWSNFK EQVYSTFDWG
IRDADGYYFI LGRTDDVINV AGHRLGTREI EESISSHPNV SEVAVVGVED KLKGQVAVAF
AIPKNGDALS SAEARKALEA EVMAVVDKRL GAVARPARVH FVSLLPKTRS GKLLRRSIQA
ICEGRDPGDL TTIEDPTSLQ QIRAVLADQT
//
