ID A0A0B4D9S0_9RHOB Unreviewed; 464 AA.
AC A0A0B4D9S0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KIC51303.1};
GN ORFNames=RA29_05605 {ECO:0000313|EMBL:KIC51303.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC51303.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KIC51303.1}.
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DR EMBL; JWLL01000003; KIC51303.1; -; Genomic_DNA.
DR RefSeq; WP_039683606.1; NZ_JWLL01000003.1.
DR AlphaFoldDB; A0A0B4D9S0; -.
DR STRING; 1577905.RA29_05605; -.
DR OrthoDB; 9811261at2; -.
DR Proteomes; UP000031171; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000031171}.
FT DOMAIN 40..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 464 AA; 52121 MW; BC8037EDF095B87E CRC64;
MNLDAAKADL AHLDIEEKEA SIRASSRDFF WYSPVLKDRL DHVVADFVVR PRNEAEVIEV
LKVCYQHDVP VTTRGAGTGN YGQAMPLEGG CVMHLRWMDK VKEVHPGRVI VEPGCLLKDL
DAVCKEQSGQ EIRMFSSTWA TATIGGFIAG GSGGVGSCTW GSLRDLGNII RLRVVTMEEE
PRILEFTGEE LARVSHAYGT NGIITEIEMP LAPAYDWVEM FVSSKDFMAA TRFAQDVANE
DGILIKLATV FEAPVAKDYF QRVAPHVEAD DHLIGLMVAP HSMDGFQTLL GRSPELNLIY
RSDDHDWERS PGTVFEYGWN HTTLRALKAD PSITYLQVRF GYPNQLELIE KMREALSPEV
LHHLEVLKEG GKVMFAGLSL VKFTTEERLD EIIQIHEDAG AMVFNPHRYT LEEGGRQTVD
DRQLKFKREA DPKGLLNPGK MIAWDDPDFD FSEMYSYPKI QAAE
//
