ID A0A1Y2K907_9PROT Unreviewed; 625 AA.
AC A0A1Y2K907;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative propionyl-CoA synthetase {ECO:0000313|EMBL:OSM07231.1};
GN Name=prpE {ECO:0000313|EMBL:OSM07231.1};
GN ORFNames=MAIT1_03838 {ECO:0000313|EMBL:OSM07231.1};
OS Magnetofaba australis IT-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetofaba.
OX NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM07231.1, ECO:0000313|Proteomes:UP000194003};
RN [1] {ECO:0000313|EMBL:OSM07231.1, ECO:0000313|Proteomes:UP000194003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT-1 {ECO:0000313|EMBL:OSM07231.1,
RC ECO:0000313|Proteomes:UP000194003};
RX PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT "Combined genomic and structural analyses of a cultured magnetotactic
RT bacterium reveals its niche adaptation to a dynamic environment.";
RL BMC Genomics 17:726-726(2016).
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:OSM07231.1}.
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DR EMBL; LVJN01000015; OSM07231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2K907; -.
DR STRING; 1434232.MAIT1_03838; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000194003; 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; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Reference proteome {ECO:0000313|Proteomes:UP000194003}.
FT DOMAIN 5..58
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 61..447
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 511..587
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 625 AA; 69444 MW; 56AD139852C3F79C CRC64;
MRARYESFFR RSLDEREAFW REQAELIHWE KPFDQVCDDS KLPFANWFVG GTTNLCYNSV
DRHLAERADQ PAIIWVSTEQ EREEKITYRQ LHEQVNALAA VLQEQGVVKG DRVLIYMPMI
PEALVAMLAC VRLGIIHSVV FGGFASHALA SRIDDAKPKM VITADAGLRG GKAVNYKPLL
KKGMNEAMAD APMVLTVNRG VATEAVEIPG ELDYATEMAK HAGAVVDPVW VESSHPSYIL
YTSGTTGKPK GVQRDTGGHA VAMRASLKHI YGVEPGETMF SGSDIGWVVG HSYIVYAPLL
TGATTIVYEG LPIRPDPGIW WRIVQDHKVN CLFTSPTAIR LLKKSGEEWI HKYDLSSMRS
LFLAGEPLDK ETHRWVMDAL KCPVVDNYWQ TETGWPILTN FMGLGLMELK HGSPSLPAYG
YDVILVDEQT AQPVGPNQKG SLMIRPPLPP GCMTTVYGDD ERFVSTYFSR FKEPLYATFD
YAMYDEDGYY FIMGRDDDVI NVAGHRMGTR EVEEALCLHP AVAEAAAVGI KDEIKGQEIE
AFVVLMANVE PPTTDELRQS VARELGPIAK PKYLHIVTSL PKTRSGKVIR RAIQSLAEGG
DPGDLPTIED ATVLDQIRGA VKDRS
//
