ID A9HAH8_GLUDA Unreviewed; 463 AA.
AC A9HAH8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=Putative deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:CAP54694.1};
GN Name=phrB {ECO:0000313|EMBL:CAP54694.1};
GN OrderedLocusNames=GDI0751 {ECO:0000313|EMBL:CAP54694.1};
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP54694.1, ECO:0000313|Proteomes:UP000001176};
RN [1] {ECO:0000313|EMBL:CAP54694.1, ECO:0000313|Proteomes:UP000001176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC PAl5 {ECO:0000313|Proteomes:UP000001176};
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1};
CC -!- SIMILARITY: Belongs to the DNA photolyase family.
CC {ECO:0000256|RuleBase:RU004182}.
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DR EMBL; AM889285; CAP54694.1; -; Genomic_DNA.
DR RefSeq; WP_012223414.1; NC_010125.1.
DR AlphaFoldDB; A9HAH8; -.
DR KEGG; gdi:GDI0751; -.
DR OMA; WQQELAW; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000001176; Chromosome.
DR GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455:SF9; (6-4)-PHOTOLYASE, ISOFORM A; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|RuleBase:RU004182};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}; Lyase {ECO:0000313|EMBL:CAP54694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001176}.
FT DOMAIN 7..132
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 230
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 242..246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 372..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 306
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 359
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 382
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 463 AA; 52142 MW; 8DF831D96D1A2674 CRC64;
MVNLAPAPTI VWFREDFRIA DNMALLEAEK RGQPTLCIVI LDDAHLPGAA ARWWLHGAIR
SLDETLRGMG GALHVFRGAA RAVLAEIVRK TGAGAVFWNR RYDPAGREAD TAIKADLRAR
GLTVRSFPGA LLHEPWSVCT RSVAPYKIFT AFWRAACALP APFPPHPAPE RLVFAPPPPM
PDSLITRHEQ DGLLPRHPDW AGGLRDMWSP GEEEAGDQLS DFLRHDGAGY ATARDFPGDE
ATSRLSPFLR FGHVSPAQVW HAATRKACPD KFLMELGWRD FAWSLLFFNP DLATRNLRPE
FDAMPWRHDP GGLAAWQRGQ TGYPLVDAGM RELWHTGWMH NRVRMVAASF LVKHLLIDWR
EGERWFADTL VDHDPASNPM NWQWNAGTGV DAAPYFRVMN PILQSRKFDP HGVYIRRWVP
ELAHLSDDAI HAPWESGATH PYPAPIVDHR AARERALAAW KMI
//