ID E6THF9_MYCSR Unreviewed; 547 AA.
AC E6THF9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Predicted kinase, dihydroxyacetone kinase {ECO:0000313|EMBL:ADU00167.1};
GN OrderedLocusNames=Mspyr1_35560 {ECO:0000313|EMBL:ADU00167.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADU00167.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU00167.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
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DR EMBL; CP002385; ADU00167.1; -; Genomic_DNA.
DR RefSeq; WP_013472153.1; NC_014814.1.
DR AlphaFoldDB; E6THF9; -.
DR KEGG; msp:Mspyr1_35560; -.
DR HOGENOM; CLU_017496_0_1_11; -.
DR Proteomes; UP000008916; Chromosome.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR InterPro; IPR033470; FakA-like_C.
DR InterPro; IPR048394; FakA-like_M.
DR InterPro; IPR019986; YloV-like.
DR NCBIfam; TIGR03599; YloV; 1.
DR PANTHER; PTHR33434; DEGV DOMAIN-CONTAINING PROTEIN DR_1986-RELATED; 1.
DR PANTHER; PTHR33434:SF4; PHOSPHATASE PROTEIN-RELATED; 1.
DR Pfam; PF02734; Dak2; 1.
DR Pfam; PF13684; FakA-like_C; 1.
DR Pfam; PF21645; FakA-like_M; 1.
DR SMART; SM01121; Dak1_2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADU00167.1};
KW Transferase {ECO:0000313|EMBL:ADU00167.1}.
FT DOMAIN 9..209
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 547 AA; 55215 MW; 87C5AA68552305EF CRC64;
MSARRLDAST LRRWAHDAVA ALISHTDEIN RLNVFPVADA DTGTNMLFTM RAAWAQADSD
AADDVTAITA ALAAGALRGA RGNSGVILSQ ILRALAEVTA EAAEERGGVL SEVTGEMLAA
ALRHAVTLVV ASMGEAVPGT IVSVLHDAAA AAEDAVCGQA DLAAVVVACT QAAAAALDRT
PTQLDVLADA GVVDAGGRGL LVLLDALSAI LTGELTRRQV YLPDPKHAAG AAAPPSPTPG
FEVMYLLSDC DAENVEQLRA RLDALGDSVA IAASGFGEAG AGHYSVHVHA DDAGAAVEAG
LAVGTLSRIQ ITSLHGGADR SSAGSWGRER AVLALVDGEG AEELFVGEGA AVLRTEPGVE
ISAQQLLHAL VKTGAAQVMV LPNGYVAAEE IVAGCAVAAD WGIDLVPIPT GSMVQGLAAL
AVHDPGHRLV DDGYTMARAG AAARFGSVRI AAEDALTWAG ACRPGDGLGI TGDEVVVVGD
DIVSAATGLI DLLLAAGGEL VTVLTGDGVE SEVGAALAEH VHHNHLGAEL VTFHTGHRAD
ALLIGVE
//
