ID A0A0H1BJW2_9EURO Unreviewed; 563 AA.
AC A0A0H1BJW2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=medium-chain acyl-CoA ligase {ECO:0000256|ARBA:ARBA00039009};
DE EC=6.2.1.2 {ECO:0000256|ARBA:ARBA00039009};
GN ORFNames=EMPG_09767 {ECO:0000313|EMBL:KLJ11292.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ11292.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000256|ARBA:ARBA00036212};
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:KLJ11292.1}.
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DR EMBL; LDEV01001646; KLJ11292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1BJW2; -.
DR STRING; 2060906.A0A0H1BJW2; -.
DR OrthoDB; 589104at2759; -.
DR Proteomes; UP000053573; Unassembled WGS sequence.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 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:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000053573}.
FT DOMAIN 24..392
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 461..543
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 563 AA; 62419 MW; D26DBD6523BDC9D4 CRC64;
MALPIPKELP PCPEYFNFAY DVVDKWAAQS PSPQAMLWVD QHGKNPLSLD FAYFSRQSNR
AAELLVQLGA RRGDRMIIVL PRVPAWWEIA TAAIRIGVVV CPCPVLAVAH DIKYRAEASK
ASIFVGDTLS ISKFKTIQRE CPDIRTIIQA TGSPLEGVLQ YSAELDSRIP RNAVFKDVLP
KTKWSDPSVI YFTSGTTGMP KMVLHNQVSY PLAHVSTGSL WLGLEPGKLY WNLSEQGWAK
AAWAWFGAWS CGAALFVQET VGPFNAESAL DNLHNYPITT LCSPPTAYRQ FVLPARRKYF
SQRPPMALEQ CVGAGEPLND EVIRIWNEMS GIEIRDGYGQ TETTLVCGNL KGGKIKYGSM
GLPVPGVPLS VVDEKGDESP PFEEGEIAIA TTTSSGARTI NVFSGYMSPD GRVTLPQRQG
KSCSWYLTGD RAYKDEDGYL WFVGRSDDVI NSSGYRIGPF EVESVLKKHP AVIESAVVAS
PDPDRVEVVK AFIVLQEEFK SRNPDSLIAE LQEFCKKETA PYKYPRRIQF VEPSFLPKTI
SGKIKRAELR ALEKVLVTRG AKI
//
