ID E6ZK34_SPORE Unreviewed; 732 AA.
AC E6ZK34;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Related to Acetoacetyl-CoA synthetase {ECO:0000313|EMBL:CBQ67687.1};
GN ORFNames=sr11637 {ECO:0000313|EMBL:CBQ67687.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ67687.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ67687.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311430; CBQ67687.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZK34; -.
DR EnsemblFungi; CBQ67687; CBQ67687; sr11637.
DR VEuPathDB; FungiDB:sr11637; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_3_1; -.
DR OrthoDB; 45466at2759; -.
DR Proteomes; UP000008867; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 44..102
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 149..532
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 732 AA; 80426 MW; 87801BE00B14D1CC CRC64;
MTTPTPAPSQ PLVWSPTPDE IQRTSLDKFR RVVNARFNLE LNSYDDLHDF SISRMEDFWA
TVWDFAGIRA STRFERVLSD PEALPGDLPE WFPGASFSMA QNVLFPLHPA NTTFCSPKAP
YHWPHAQAVA LIEVPEGGGL AGSDANAQAV KVTWGELRRR VALLAETFRR IGVKKGDRLA
HVSANTASPI VATLAANSVG AIYSLIATDA GPQAIYGRLA QIRPKLLFTD DAVLYNGKQV
DILDRVAHVA ERLQADDKID SPLSFQVVII RNARLPNTSP RWTSTKVRGL EMDAFITQTG
LHMGDSPAHR FEQLRAQHPV QIFFSSGTTG EPKCIIHTQC MLLNMKKEAL LMMDLQPADT
FLQITSCGWI MWLYHLVALS VGSTAVLYDG SPMFPNPAHV VKVVSHLKCS GYGASPRFLS
ELEKFCAENR FSIARQLELG KFRMMTSTGS PLSPKNVDFF YSHFPKRAHL CSISGGTDMA
GVLVGPTKML PLYGNFIQCK ALGFDIQVWD AETGERIDET GKPGELIVAK PFPTQLQALY
EKYMDSYYAR FPGRKVWAQG DFIYQDTATK GLEILGRSDG VLNPSGVRFG SSEIYSVVEK
FEFVGDSIVV GQRRPGKDEH ERVLLFIKMR DPAATLDGTH IAQLNSAIKA AYSARHVPEH
TFQVHDIPVT LNGKKTELAV KAVVNGNAAF KPSSATANPQ SLAEYAQYAD LEAVVAARSG
ARAGAARGGA KL
//
