ID A0A094CS37_9PEZI Unreviewed; 563 AA.
AC A0A094CS37;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=medium-chain acyl-CoA ligase {ECO:0000256|ARBA:ARBA00039009};
DE EC=6.2.1.2 {ECO:0000256|ARBA:ARBA00039009};
GN ORFNames=V496_09541 {ECO:0000313|EMBL:KFY50180.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY50180.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY50180.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY50180.1}.
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DR EMBL; JPJY01001871; KFY50180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CS37; -.
DR STRING; 1420909.A0A094CS37; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR OrthoDB; 589104at2759; -.
DR Proteomes; UP000029302; 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:UP000029302}.
FT DOMAIN 24..385
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 462..544
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 563 AA; 62965 MW; D31F14850776E857 CRC64;
MAHFYDSVLQ RPDSFNFAVD VVDYWAAQPG DLEAMYWVSQ DEFQKRSLTF KYFSRQSHRV
SVLLQRLGVK EGETVVMVVP RVPAWWEIAV GAIRSGIIIA PATTLLTAKD IQYRCAKSKA
SVFVGDGASV AKFLTVRDEC SSVRTILQVG DVIHPGASSF YASLELVEAD ASVEDVRRDW
NSPSLIYFTS GTSGPPKMVC HNQVSYPLAL TTTAKSWYQL APGKVLWNTA EQGWGKAAWS
FFGAWNCGAT LFVYDDRGPF SAQRLLRILH QYPITTICAA PLAFRQLVLQ EAKSYYEKYP
PMALSHCTAA GEALNDEVIR QWHAISGMEI RDGYGQTETI LLCGNFSGFA IRPGSMGKPA
PTVPLSIING DGSETVAGEE GDIAVLLDNI SCKKDFFGLF DGYLNEDSTV SRREKIFTKN
GERKVWYLTG DKARRDEDGY FWFVGRSDDV INSSGYRIGP FEVESTLKLH PSVVESAVIS
SPDPVRGEVV KAFVVLTEQW KDVNQDLLKK ELQDFCKKNA APYKYPRKIQ FVPSNFLPRT
ASGKIQRNEL RKMEWKSETK AKL
//
