Comparing RR42_RS01370 FitnessBrowser__Cup4G11:RR42_RS01370 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
P55882 Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; Hydroxymethylpyrimidine kinase; HMP kinase; Hydroxymethylpyrimidine phosphate kinase; HMP-P kinase; HMP-phosphate kinase; HMPP kinase; EC 2.7.1.49; EC 2.7.4.7 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
48% identity, 94% coverage: 12:271/276 of query aligns to 7:264/266 of P55882
7r8yA Ancestral protein ancthen of phosphomethylpyrimidine kinases family
58% identity, 90% coverage: 6:253/276 of query aligns to 1:228/228 of 7r8yA
Q5M731 Thiamine biosynthetic bifunctional enzyme TH1, chloroplastic; EC 2.5.1.3; EC 2.7.1.49 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 97% coverage: 2:270/276 of query aligns to 24:292/522 of Q5M731
1jxiA 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase from salmonella typhimurium complexed with 4-amino-5- hydroxymethyl-2-methylpyrimidine (see paper)
45% identity, 94% coverage: 12:271/276 of query aligns to 7:252/254 of 1jxiA
7l07A Last common ancestor of hmppk and plk/hmppk vitamin kinases (see paper)
44% identity, 89% coverage: 3:249/276 of query aligns to 1:214/214 of 7l07A
2i5bA The crystal structure of an adp complex of bacillus subtilis pyridoxal kinase provides evidence for the parralel emergence of enzyme activity during evolution (see paper)
40% identity, 94% coverage: 10:269/276 of query aligns to 3:261/269 of 2i5bA
4c5kD Structure of the pyridoxal kinase from staphylococcus aureus in complex with adp (see paper)
39% identity, 96% coverage: 10:274/276 of query aligns to 5:266/276 of 4c5kD
4c5mA Structure of the pyridoxal kinase from staphylococcus aureus in complex with amp-pcp (see paper)
39% identity, 96% coverage: 10:274/276 of query aligns to 5:263/273 of 4c5mA
4c5lB Structure of the pyridoxal kinase from staphylococcus aureus in complex with pyridoxal (see paper)
39% identity, 96% coverage: 10:274/276 of query aligns to 5:261/271 of 4c5lB
4c5lA Structure of the pyridoxal kinase from staphylococcus aureus in complex with pyridoxal (see paper)
38% identity, 96% coverage: 10:274/276 of query aligns to 5:254/264 of 4c5lA
4ywrA Structure of a putative phosphomethylpyrimidine kinase from acinetobacter baumannii in non-covalent complex with pyridoxal phosphate
37% identity, 84% coverage: 9:241/276 of query aligns to 2:218/228 of 4ywrA
P40191 Pyridoxine/pyridoxal/pyridoxamine kinase; PN/PL/PM kinase; B6-vitamer kinase; Pyridoxal kinase 1; PL kinase 1; EC 2.7.1.35 from Escherichia coli (strain K12) (see paper)
27% identity, 59% coverage: 80:243/276 of query aligns to 91:256/283 of P40191
Sites not aligning to the query:
3mbhA Crystal structure of a putative phosphomethylpyrimidine kinase (bt_4458) from bacteroides thetaiotaomicron vpi-5482 at 2.00 a resolution (orthorhombic form with pyridoxal)
26% identity, 70% coverage: 75:266/276 of query aligns to 74:270/290 of 3mbhA
Sites not aligning to the query:
2ddwA Crystal structure of pyridoxal kinase from the escherichia coli pdxk gene complexed with pyridoxal at 3.2 a resolution (see paper)
27% identity, 59% coverage: 80:243/276 of query aligns to 82:239/263 of 2ddwA
Sites not aligning to the query:
2ddoA Crystal structure of pyridoxal kinase from the escherichia coli pdxk gene at 2.6 a resolution (see paper)
27% identity, 59% coverage: 80:243/276 of query aligns to 82:239/263 of 2ddoA
Sites not aligning to the query:
>RR42_RS01370 FitnessBrowser__Cup4G11:RR42_RS01370
MTLTTHRPPRTLTIAGSDSGGGAGIQADLKTFAALGCFGMSAITAITAQNTLGVTGVHAI
PADMVAAQIDAVASDIGVDAAKTGMLGTAAIVEAVAAAVDRHGIRQLVVDPVMISTSGAT
LADDATTQAMVRLLFPRAVLVTPNLPEASYLLGREITRREEMEQAARDLAALGCPAVLLK
GGHLDPADAGLDDLLLSADGTVRVFRHQRVDTRNLHGTGCTLAAAIAAQLARGDKVEDAV
EVALDFVADAIVAGADFALGTGNGPLNHGFAPRVLG
Or try a new SitesBLAST search
SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory