ACL_RS05470

Uniprot: A9NH86
Description: bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase
EC number:
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity:
Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-3}; ; Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-3}
Enzyme regulation:
Function [CC]: FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate. {ECO:0000256|PIRNR:PIRNR006769}.
Pathway: PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4. {ECO:0000256|PIRNR:PIRNR006769}.; PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4. {ECO:0000256|PIRNR:PIRNR006769}.
Active site: ACT_SITE 55 55 Proton donor. {ECO:0000256|PIRSR:PIRSR006769-1}.
Binding site: BINDING 157 157 NADP; via amide nitrogen and carbonyl oxygen. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 171 171 Substrate. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 173 173 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 187 187 Substrate. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 199 199 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 203 203 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 207 207 Substrate; via amide nitrogen. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 210 210 Substrate. {ECO:0000256|PIRSR:PIRSR006769-2}.; BINDING 288 288 Substrate. {ECO:0000256|PIRSR:PIRSR006769-2}.
Calcium binding:
DNA binding:
Metal binding: METAL 53 53 Zinc; catalytic. {ECO:0000256|PIRSR:PIRSR006769-3}.; METAL 78 78 Zinc; catalytic. {ECO:0000256|PIRSR:PIRSR006769-3}.; METAL 87 87 Zinc; catalytic. {ECO:0000256|PIRSR:PIRSR006769-3}.
Nucleotide binding: NP_BIND 290 296 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
Site:
Gene names (primary): ribD
Gene names (synonym):
Mass: 39,750
Subunit structure [CC]:
Gene ontology (GO): 5-amino-6-(5-phosphoribosylamino)uracil reductase activity [GO:0008703]; diaminohydroxyphosphoribosylaminopyrimidine deaminase activity [GO:0008835]; NADP binding [GO:0050661]; zinc ion binding [GO:0008270]; riboflavin biosynthetic process [GO:0009231]
Gene ontology IDs: GO:0008270; GO:0008703; GO:0008835; GO:0009231; GO:0050661
Chain:
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: In the C-terminal section; belongs to the HTP reductase family. {ECO:0000256|PIRNR:PIRNR006769}.; SIMILARITY: In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family. {ECO:0000256|PIRNR:PIRNR006769}.
Protein families: HTP reductase family; Cytidine and deoxycytidylate deaminase family
Coiled coil:
Domain [FT]: DOMAIN 4 126 CMP/dCMP-type deaminase. {ECO:0000259|PROSITE:PS51747}.
Motif:
Region:
EMBL: CP000896
ProteinModelPortal: A9NH86
MEROPS:
EnsemblBacteria KO: ABX81716
UniPathway: K11752
CDD:
Gene3D:
HAMAP: 3.40.430.10
InterPro:
PANTHER: IPR016192;IPR002125;IPR016193;IPR024072;IPR004794;IPR011549;IPR002734
PIRSF:
PRINTS: PIRSF006769
PROSITE:
Pfam: PS00903;PS51747
ProDom: PF00383;PF01872
SMART:
SUPFAM:
TIGRFAMs: SSF53597;SSF53927

1142832-1143906(-)

>nucleotide sequence
TTATTTAAAATAACCTTCAATTAAGATGTCCTCATCAAATTGTGTATAAGTAACATCTTT
TAATACATGGGCATCTTTCATTAAAGATACACCTTCCCCACCTATTGGAGTAAGTGCATT
TTTTCCACCTATGATTTTAGGTGCTATAAATGCATAAACTTTATTCACTAAATTAGCTTC
TAAGAAACTCGCATGCGTATATGCACCACCCTCAATGAAGATACTATCTATTTTTGCTTC
ACCTAGAATCGTCATAAGCTTATCTAAATCAATGGTTGGCATTTGAATGATTTTAACACC
CAAATCCACATAGCTTTGATCATATGTTTCAGAGACTATCCAAGTTGGTTGGGTTTTAGC
TGTTTTTACAACATAAGTACTCTTTGGTGTTTGTAGTTTTGGGTCTAAGATTATTCTTAC
TGGGTTTTTAGATTTCTTACTTCTTCTAACATCGAGTTTTGCATCATCTTTAATGATTGT
GTTCACACCAACAAGTATTGCACTATATTTATTTCTTAAATCATGAACATATTTTCTTGA
TTTTTTATTAGTTATCCATTTAGAATCAAAATCTTTAGTTGCTAATTTACCATCTAAAGT
CATGGCATACTTCATGGCTACAAATGGTCTTTTAGTTGTAATATAGTGAAAGAATATATC
GTTTACTTTTAAACCTAGGTCATCTAAGATACCATAATGTACTTTGATGCCGGCATCTTC
TAGCACTTTAACGCCTTGTTTATAGACTAGTGGGTTTGGATCTAAGTTTGCAATATAAAC
TTCTTTAATACCTTTTTCTATCAGTTTAAATGCACACGGTGGTTGTTTACCATGGTGACT
ACATGGTTCTAGTGTTACAAACATCGTTGCACCAGCTACATCTTCTGTTGCATGATTAAT
TGCATCCACTTCAGCGTGTACTTGACCAAATGCCTTATGATACCCTTTACCAATGACCTT
ACCATCTTTAATGATAACCGCACCAACAAGTGGGTTTGGATTCACAAATCCTTCGCCTTT
TATTGCTAAATTAAACGCTTGTTTCATGTATTTCGTCTGTAATTTTAAGTCCAT

>protein sequence
MDLKLQTKYMKQAFNLAIKGEGFVNPNPLVGAVIIKDGKVIGKGYHKAFGQVHAEVDAIN
HATEDVAGATMFVTLEPCSHHGKQPPCAFKLIEKGIKEVYIANLDPNPLVYKQGVKVLED
AGIKVHYGILDDLGLKVNDIFFHYITTKRPFVAMKYAMTLDGKLATKDFDSKWITNKKSR
KYVHDLRNKYSAILVGVNTIIKDDAKLDVRRSKKSKNPVRIILDPKLQTPKSTYVVKTAK
TQPTWIVSETYDQSYVDLGVKIIQMPTIDLDKLMTILGEAKIDSIFIEGGAYTHASFLEA
NLVNKVYAFIAPKIIGGKNALTPIGGEGVSLMKDAHVLKDVTYTQFDEDILIEGYFK