ID K2SAL9_MACPH Unreviewed; 481 AA.
AC K2SAL9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ketose-bisphosphate aldolase class-II family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MPH_08929 {ECO:0000313|EMBL:EKG13930.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG13930.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG13930.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG13930.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000256|ARBA:ARBA00005715}.
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:EKG13930.1}.
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DR EMBL; AHHD01000378; EKG13930.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SAL9; -.
DR STRING; 1126212.K2SAL9; -.
DR VEuPathDB; FungiDB:MPH_08929; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_044742_0_0_1; -.
DR InParanoid; K2SAL9; -.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.980.20; Four-carbon acid sugar kinase, nucleotide binding domain; 1.
DR Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR InterPro; IPR010737; 4-carb_acid_sugar_kinase_N.
DR InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
DR InterPro; IPR031475; NBD_C.
DR InterPro; IPR042213; NBD_C_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF17042; NBD_C; 1.
DR Pfam; PF07005; SBD_N; 1.
DR SUPFAM; SSF142764; YgbK-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 43..281
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 305..471
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 481 AA; 51069 MW; 0BB91E9E848CB51A CRC64;
MATPPQPLPL DSTLSSLPPI HPGDLRAQTR ALLAANAASI PLLVALDDDP TGTQTCHDIR
VLTVWDVATL AAELASTPPG SGFFILTNSR ALHAPEARAL VAEICANLRA AAEQAARAFE
VVLRGDSTLR GHFPEEPEVV DEVLGGSDAW VLAPFFLQGG RYTIGDVHYV AEGDTLVPAG
ETPFARDATF GYASSDLRDW VVEKTGGKIA RERVVSLGLQ DIREGGPERI VELVEGFEKG
SIIVVNAAAE EDMDVVVLGL LKASSTGKRF LFRTAAAFVS ARLGISPIAP ISAQQLQLSR
EAGGLIIAGS YVPKTTAQLE VLTSKSGDKL KTVVMDVEKL LASPESAAEV IAHAIAVAEK
EIAQRQDVLI MTSRKLVVGD DAKKSLDIGS VVADALVKFM QQLKVKPRYV IAKGGITSSD
MATKGLNMKK ATIVGQAAPG IPLWRCDEET CKYPGLPYVV FPGNVGSTET LYDVVEGWRV
S
//
