ID D4B5D9_ARTBC Unreviewed; 278 AA.
AC D4B5D9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Macrophomate synthase, putative {ECO:0000313|EMBL:EFE29472.1};
GN ORFNames=ARB_03679 {ECO:0000313|EMBL:EFE29472.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE29472.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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:EFE29472.1}.
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DR EMBL; ABSU01000039; EFE29472.1; -; Genomic_DNA.
DR RefSeq; XP_003010112.1; XM_003010066.1.
DR AlphaFoldDB; D4B5D9; -.
DR STRING; 663331.D4B5D9; -.
DR GeneID; 9525380; -.
DR KEGG; abe:ARB_03679; -.
DR eggNOG; ENOG502QR7H; Eukaryota.
DR HOGENOM; CLU_059964_3_0_1; -.
DR OMA; WNRVDDY; -.
DR OrthoDB; 2785075at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 31..263
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
SQ SEQUENCE 278 AA; 29795 MW; 17713315436FD1F4 CRC64;
MAATMQAANR LQSVLKAGKT AYGVWQMFPG ANLSRVMARC GFDWVLVDTE HGNIDDAQMH
EAVGAIAATG VSPVVRIAAN EGWMVKRMFM VNTAFITGEM DTDGSEIGAL DAGAHGILVP
LLETADDARK LVQSAKFPPV GKRGFGAPFA MGSIGNVSPI EYLQHANDAL ITAVQIETKS
ALDNVEEIAR VPGVDVLLVG PWDLGNNIGR PVVTTEFHPD LEIAIERIRK AATDNGKKAG
IYCPSGEFAK KYIDQGFHMV RPAFPFCSLL QLRAVAVC
//
