ACL_RS07185


  Uniprot: A9NF43
Description: dephospho-CoA kinase
EC number: 3.2.2.-; 3.2.2.23; 4.2.99.18
Annotation score: 3 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. {ECO:0000256|SAAS:SAAS00020866}.; CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. {ECO:0000256|SAAS:SAAS00557314}.
Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|SAAS:SAAS00610166};
Enzyme regulation: 
Function [CC]: FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. {ECO:0000256|SAAS:SAAS00348515}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): 
Gene names (synonym): 
Mass: 51,823
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|SAAS:SAAS00020849}.
Gene ontology (GO): ATP binding [GO:0005524]; damaged DNA binding [GO:0003684]; dephospho-CoA kinase activity [GO:0004140]; oxidized purine nucleobase lesion DNA N-glycosylase activity [GO:0008534]; zinc ion binding [GO:0008270]; base-excision repair [GO:0006284]; coenzyme A biosynthetic process [GO:0015937]; nucleotide-excision repair [GO:0006289]
Gene ontology IDs: GO:0003684; GO:0004140; GO:0005524; GO:0006284; GO:0006289; GO:0008270; GO:0008534; GO:0015937
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the CoaE family. {ECO:0000256|SAAS:SAAS00580898}.; SIMILARITY: Belongs to the FPG family. {ECO:0000256|SAAS:SAAS00557294}.; SIMILARITY: Contains DPCK (dephospho-CoA kinase) domain. {ECO:0000256|SAAS:SAAS00515713}.; SIMILARITY: Contains FPG-type zinc finger. {ECO:0000256|SAAS:SAAS00551694}.
Protein families: CoaE family; FPG family
Coiled coil: 
Domain [FT]: DOMAIN 2 109 FPG_CAT. {ECO:0000259|PROSITE:PS51068}.; DOMAIN 232 266 FPG-type. {ECO:0000259|PROSITE:PS51066}.
Motif: 
Region: 
EMBL: CP000896
ProteinModelPortal: A9NF43
MEROPS: 
EnsemblBacteria KO: ABX80973
UniPathway: K10563
CDD: 
Gene3D: 
HAMAP: 3.40.50.300
InterPro: MF_00376
PANTHER: IPR001977;IPR015886;IPR015887;IPR020629;IPR012319;IPR027417;IPR010979;IPR000214;IPR010663
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: PS51219;PS51068;PS01242;PS51066
ProDom: PF01121;PF01149;PF06831;PF06827
SMART: 
SUPFAM: SM00898;SM01232
TIGRFAMs: SSF46946;SSF52540;SSF81624
368411-369770(+)

>nucleotide sequence
ATGCCTGAACTACCTGAGGTAGAAACCATTCGTAGAAATTTAAATACAGTATTAGAAGGT
GAAATCATACGTGAGGTTTTAGTATACTATCGACCTATTGTTTCAAATGATGCGTCATTT
GAAACCAAATTAAAAGGTCAACGTATACATAAAGTAGAACGTGAAGCAAAGTATTTAAAG
TTTATTTTAGATGACTATCTTTTAGTATCTCATTTACGTATGGAAGGCAAATACTTTATG
GACGCGCCTTTAAATAAACATATACATGTAGTGTTTAATCTATCAAGCGGTCACACGTTA
AGTTATGAAGATACACGTAAATTTGGCCGTTTTGAACTGGTAGATATTAAATATAAAGAC
ACTTATTTAAAAGATATTAAAGGGCTTGCTAAAGACCCTGATACCCTAGATTTAAACACC
TTTTATAGTAGTTTTAATCAAAGAAGTAAAACGATTAAAGAAATATTACTGGATCAATCC
ATTATTGGTGGTATTGGTAATATTTATGCAAATGAAATACTTTACTTATCTAAAATACAT
CCAGCCAAAAAAGGTTTTTTAATCAGTAAAGATGAAGCAAAAACCTTACTAAATAACTCT
AATCTTGTTTTAAACAAGGCCATCGAAATGGGTGGAACGACAATTGACACCTTTGAATCA
TTAGGGCATAAGGGTGAGTTTCAACAGGAGTTAAATGTTCATGGCAAAACTGGAGAGATT
TGTAAGGTATGTGGCACTAAAATAATTAAATTTCAGTTAAAAGGACGAGGTACTTATATT
TGTCCTAAATGCCAACCATCTTATGTAGTCGCAATCACAGGTGGTATTGCAACCGGTAAA
TCTACTGCAACAAACTATTTAAGAAAAAAAGGATTTGTAGTTGTAGATTCTGATGAAATT
GTAGGAAGTCTTTATCAAGATAGTGATGTACTAAATTTAATTGCAAAAACCTTTAAAATG
GAAACACCAATTGATAAAGCAAAACTTGCAAACATCGTTTTCCATGATGAAAAACAAAGA
AAAAAATTAGAACACATCTTACATCCACTCGTTTTTGATGAAATTAGCAAACAAAAACAA
TTAAATAATGAACATATCTTATTTTTAGATATTCCTTTATTATTTGAATCGAATTACAAA
GAGTTTGATGAATCCATCTTAATAGATACAACTGAAGCACTTCAACTGGATAGATTAATG
AAGCGCAACAAATATACTCAAGAAGAAGCACTTGTTCGTATAAAAGCGCAGATACCTTTA
AGTAAAAAGCGCAAACTAGCTACACACATTATAAAAAATAATGGATCTATAGATGCGTTA
TATGAAAAAATAGATAAATTATTAGAAAGGTATGTATAA


>protein sequence
MPELPEVETIRRNLNTVLEGEIIREVLVYYRPIVSNDASFETKLKGQRIHKVEREAKYLK
FILDDYLLVSHLRMEGKYFMDAPLNKHIHVVFNLSSGHTLSYEDTRKFGRFELVDIKYKD
TYLKDIKGLAKDPDTLDLNTFYSSFNQRSKTIKEILLDQSIIGGIGNIYANEILYLSKIH
PAKKGFLISKDEAKTLLNNSNLVLNKAIEMGGTTIDTFESLGHKGEFQQELNVHGKTGEI
CKVCGTKIIKFQLKGRGTYICPKCQPSYVVAITGGIATGKSTATNYLRKKGFVVVDSDEI
VGSLYQDSDVLNLIAKTFKMETPIDKAKLANIVFHDEKQRKKLEHILHPLVFDEISKQKQ
LNNEHILFLDIPLLFESNYKEFDESILIDTTEALQLDRLMKRNKYTQEEALVRIKAQIPL
SKKRKLATHIIKNNGSIDALYEKIDKLLERYV






















© Fisunov Lab of Proteomics, 2016.