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Database: UniProt
Entry: K2HBS2_9RHOB
LinkDB: K2HBS2_9RHOB
Original site: K2HBS2_9RHOB 
ID   K2HBS2_9RHOB            Unreviewed;       474 AA.
AC   K2HBS2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Deoxyribodipyrimidine photolyase, putative {ECO:0000313|EMBL:EKE44057.1};
GN   ORFNames=OCGS_2038 {ECO:0000313|EMBL:EKE44057.1};
OS   Oceaniovalibus guishaninsula JLT2003.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Oceaniovalibus.
OX   NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE44057.1, ECO:0000313|Proteomes:UP000006765};
RN   [1] {ECO:0000313|EMBL:EKE44057.1, ECO:0000313|Proteomes:UP000006765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2003 {ECO:0000313|EMBL:EKE44057.1,
RC   ECO:0000313|Proteomes:UP000006765};
RX   PubMed=23144420; DOI=10.1128/JB.01874-12;
RA   Tang K., Liu K., Jiao N.;
RT   "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T.";
RL   J. Bacteriol. 194:6683-6683(2012).
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}.
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:EKE44057.1}.
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DR   EMBL; AMGO01000046; EKE44057.1; -; Genomic_DNA.
DR   RefSeq; WP_007427190.1; NZ_AMGO01000046.1.
DR   AlphaFoldDB; K2HBS2; -.
DR   STRING; 1231392.OCGS_2038; -.
DR   PATRIC; fig|1231392.3.peg.2049; -.
DR   eggNOG; COG0415; Bacteria.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000006765; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {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:EKE44057.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006765}.
FT   DOMAIN          6..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         237..241
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         374..376
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            361
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            384
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   474 AA;  53134 MW;  3A1EFE8AD0EB5785 CRC64;
     MSADAAPILL WFRRDFRLTD HPALDAAARS GRPVIPVFLN DEVVRTYGAA PTWRLGLAAE
     AFAERLKGIG SRLTFREGRA AEALARLADE TGARTVWWTR AYDPASLARD EAVKEALVAR
     GVDCADHPGH LLFEPESVRT GQDGYYKVYT PYWRKVKDRD PGPALTAPTA LQAPDGWPET
     DDPAIWGLGT AMNRGAAIVA PHCHVGEAAA QTRLAVFLRD RVEGYATARD IPAMHGTSGL
     SENLTYGEIS IRSCWHSAQR AIAEGKRGAP TFLKELVWRE FAYHLLYHTP RLITGNWRPE
     WDAFPWNEDA AGDDATAWKR GRTGMPFVDA AMREMFVTGT MHNRARMIVA SYLTKHLMCH
     WKIGMHWFEE CLIDWDPANN AMGWQWSAGS GPDATPFFRV FNPETQLDRF DADRTYIRRW
     IAEGRDDPDP CALAYFDAIP RRWGMAADDA YPDPIVTAAE GRARALDAYR GRDL
//
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