ID A0A2V3DSY6_9MICC Unreviewed; 631 AA.
AC A0A2V3DSY6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:PXA65385.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:PXA65385.1};
GN Name=prpE {ECO:0000313|EMBL:PXA65385.1};
GN Synonyms=yahU {ECO:0000313|EMBL:PXA65385.1};
GN ORFNames=CVS29_08925 {ECO:0000313|EMBL:PXA65385.1};
OS Arthrobacter psychrochitiniphilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=291045 {ECO:0000313|EMBL:PXA65385.1, ECO:0000313|Proteomes:UP000246303};
RN [1] {ECO:0000313|EMBL:PXA65385.1, ECO:0000313|Proteomes:UP000246303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP3 {ECO:0000313|EMBL:PXA65385.1,
RC ECO:0000313|Proteomes:UP000246303};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-2018) 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:PXA65385.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QHLZ01000005; PXA65385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3DSY6; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000246303; Unassembled WGS sequence.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
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 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:PXA65385.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246303}.
FT DOMAIN 8..62
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 66..452
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 517..595
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 631 AA; 67772 MW; 4BED0256975E1D89 CRC64;
MAHNGTSYQD EYQRSIDDPE GFWLEAAQAL DWVVAPQQAH SDVDAPLSRW FPDGEMNTSY
NALDRHVAAG RGDQIALIHD SAMRETITRY TYNELLAAVA SFAGVLRAQG VGKGDRVIIY
LPMIPEAAIA MLAAARLGAI HSVVFGGFAA SELAMRIKDA APKVIITTSG GLEPNRKVEY
LPTVREALEK AGVPALPVVI KHRDGFATQP ADLGFNAVDW DTALAAAVPA APVTLKSTDP
LYVLYTSGTT GTPKGVVRDN GGHAVALLWT MANLYDIHAG DIWWTASDVG WVVGHSYIVY
GPLLAGATTL MYEGKPVGTP DAGAFWRVIA EHGVKALFTA PTAIRAIRKM DPEAVLLKKY
SLGTLQTLFT AGERLDSDTY HWASRVLEVP VVDHWWQTET GWGIVGNPRG LDPLPIKAGS
PTLPMPGYQL EIVDGMGVPV GAGEEGNIVL RLPLPPGTLT TLWGDDQRFV DSYLSAFTGY
YATGDSGYVD QDGYVFVMGR TDDVINVAGH RLSTGAIEQV VGKHPAVAEC AVIGVADVLK
GQKAVGYIVL KSGVSITQEQ LQLELVALVR KEIGPVADFR KAIIVDALPK TRSGKILRKT
MRQIADGNDY VVPSTIEDGS VIEALIPFLR G
//
