ID A1DMP5_NEOFI Unreviewed; 593 AA.
AC A1DMP5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=glycerol kinase {ECO:0000256|ARBA:ARBA00012099};
DE EC=2.7.1.30 {ECO:0000256|ARBA:ARBA00012099};
GN ORFNames=NFIA_054120 {ECO:0000313|EMBL:EAW16066.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16066.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005190}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU003733}.
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DR EMBL; DS027698; EAW16066.1; -; Genomic_DNA.
DR RefSeq; XP_001257963.1; XM_001257962.1.
DR AlphaFoldDB; A1DMP5; -.
DR STRING; 331117.A1DMP5; -.
DR EnsemblFungi; EAW16066; EAW16066; NFIA_054120.
DR GeneID; 4584478; -.
DR KEGG; nfi:NFIA_054120; -.
DR VEuPathDB; FungiDB:NFIA_054120; -.
DR eggNOG; KOG2517; Eukaryota.
DR HOGENOM; CLU_009281_2_2_1; -.
DR OMA; HKTDATN; -.
DR OrthoDB; 2734344at2759; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07795; FGGY_ScGut1p_like; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR NCBIfam; TIGR01311; glycerol_kin; 1.
DR PANTHER; PTHR10196:SF75; GLYCEROL KINASE; 1.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:EAW16066.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 9..261
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 271..459
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 593 AA; 65067 MW; 2E4ABB37E6FDE732 CRC64;
MQPSEIFVGS IDQGTTSSRF LIFNRDGEPV ASHQVEFTQI YPNPGWHEHD PFELVSSVET
CIEEAVKQFE SEGYSRYSVK AIGITNQRET TVVWDHETGE PLYNAIVWTD TRPQAIVHEL
KQKREASQLQ PICGLPLTTY SSATKLLWMI EHVPKVKDAY ERGTLAFGTV DAWLVYRLNG
GASANVFVSD PTNASRTMFM NLETLQYDNF LLDFFGIRGK VHLPKIVPSS DAKAYGALAS
GTLAGVPIMG CLGDQSSALV GQKGFSPGMA KNTYGTGCFL LYNVGEKPVI SEHGLLATVA
YHFDGKPVYA LEGSIAVAGS GIKFLQNNLN FFQESKEVND LAQTVEDSGG CVFVTAFSGL
YAPYWIDDAK GTMFGITQYT QKGHIARATL EATCFQTKAI LDAMEKDSGH ALSELAVDGG
MSNSDLAMQI QADLISIPVY RPKMRETTAL GAAIAAGLAV GVWRNFAELR DINRAGGAVF
EPKISREESA KSFARWEKAV AMCKGWSGDE PPPPVQPSQK EIKKNAPEVV SNHNAINATP
PKFNGELTTP KFPLISISGD LDDADEEDLY LELRKIEILQ RLKKLRKLKL SFY
//
