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Database: UniProt
Entry: V2GC92_9BURK
LinkDB: V2GC92_9BURK
Original site: V2GC92_9BURK 
ID   V2GC92_9BURK            Unreviewed;       449 AA.
AC   V2GC92;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:ESH85830.1};
GN   ORFNames=B551_0225555 {ECO:0000313|EMBL:ESH85830.1};
OS   Cupriavidus sp. HPC(L).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESH85830.1, ECO:0000313|Proteomes:UP000053474};
RN   [1] {ECO:0000313|EMBL:ESH85830.1, ECO:0000313|Proteomes:UP000053474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA   Purohit H.J., Agarwal L.;
RT   "Cupriavidus a Desert isolate.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00009410}.
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:ESH85830.1}.
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DR   EMBL; AMPR02000473; ESH85830.1; -; Genomic_DNA.
DR   RefSeq; WP_023265236.1; NZ_AMPR02000473.1.
DR   AlphaFoldDB; V2GC92; -.
DR   OrthoDB; 18526at2; -.
DR   Proteomes; UP000053474; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT   DOMAIN          15..410
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          420..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  48914 MW;  923962A1DF252068 CRC64;
     MEHQNAPIPP SRPPRVAVVG AGIVGSAIAY ELQKRGADVT LIDRDEPGQA CSYGNSGAIS
     PGSVAPLAMP GVLASLPTML LDERSPLYLP LSYLPRALPW LLRFIASASP HRVEQAAERL
     HAIHVNAVQR HRQLTQEIGA PELLMQRGHL HLYPDAGALE KDATSWRMRK EFGYDVETLG
     RAGIEALEPN VGKRYQIGVF LQDHATIVNP GRYVQAIVRA FEQRGGQRRR TEVRALRRAD
     FAGRPRWCVV EADGREDECF DEVVVAAGAW SRRLTAPLGL DLPLESQRGY HVQFRDAART
     VSRTVVLADR KVFVTPMEEG LRVGGTVEIG GLSRPPDMRR AAMLERIARE TFDGLDDPAP
     SRWMGHRPCM PDSVPIVGPA DGHPGLWLAV GHGHLGVTDS VNTAYRIADR MLEAGGDAES
     HWVPASAGTT DSAVDASFRR PREGGGPAA
//
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