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Database: UniProt
Entry: K5YTH6_9PROT
LinkDB: K5YTH6_9PROT
Original site: K5YTH6_9PROT 
ID   K5YTH6_9PROT            Unreviewed;       341 AA.
AC   K5YTH6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Hydroxylysine kinase {ECO:0000256|ARBA:ARBA00040505};
DE            EC=2.7.1.81 {ECO:0000256|ARBA:ARBA00038873};
GN   ORFNames=MXAZACID_15684 {ECO:0000313|EMBL:EKM98388.1};
OS   Acidocella sp. MX-AZ02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKM98388.1, ECO:0000313|Proteomes:UP000006217};
RN   [1] {ECO:0000313|EMBL:EKM98388.1, ECO:0000313|Proteomes:UP000006217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKM98388.1,
RC   ECO:0000313|Proteomes:UP000006217};
RX   PubMed=23405365;
RA   Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT   "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT   AZ02.";
RL   Genome Announc. 1:E00041-12(2013).
CC   -!- FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-
CC       lysine. {ECO:0000256|ARBA:ARBA00037368}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5R)-5-hydroxy-L-lysine + GTP = (5R)-5-phosphooxy-L-lysine +
CC         GDP + H(+); Xref=Rhea:RHEA:19049, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57882, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58357; EC=2.7.1.81;
CC         Evidence={ECO:0000256|ARBA:ARBA00036820};
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:EKM98388.1}.
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DR   EMBL; AMPS01000223; EKM98388.1; -; Genomic_DNA.
DR   RefSeq; WP_008495461.1; NZ_JH976210.1.
DR   AlphaFoldDB; K5YTH6; -.
DR   STRING; 1214225.MXAZACID_15684; -.
DR   HOGENOM; CLU_042971_0_1_5; -.
DR   Proteomes; UP000006217; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR21064:SF1; HYDROXYLYSINE KINASE; 1.
DR   PANTHER; PTHR21064; UNCHARACTERIZED; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:EKM98388.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW   Transferase {ECO:0000313|EMBL:EKM98388.1}.
FT   DOMAIN          44..258
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   341 AA;  36352 MW;  033889C3C409D0D3 CRC64;
     MSHQAALDLL ETPPPDIALP PILAFLAREY GLHGTLTRLP SEKDLTFGLD TGAGRDWVVK
     IANIAEPPEA LALQAAALDH LAVTAPDLGT ARVRRTLTGE VFPRIHDEAG AAHIMLVVSY
     VPGAQIGGEA LNAADAAAIG NMLAGLDRGL AGFTHKAAQR TLLWDHRRLP DYTGMMEMIA
     DPAHQALARR ALARYRAAAL PHQGALRQQI VHNDFNPYNI MRDEAGRLGV IDFGDMLQAP
     LVQDLAVALA YLVPRGEGAL GHAPSCVRAY GAMLPLTKLE QQLLPALTGA RAALTLTIAN
     WRAARNPHRA DYILRNAPSA ARALARLDAA GDEAAALLFA P
//
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