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Database: UniProt
Entry: A0A099L0Q4_9GAMM
LinkDB: A0A099L0Q4_9GAMM
Original site: A0A099L0Q4_9GAMM 
ID   A0A099L0Q4_9GAMM        Unreviewed;       392 AA.
AC   A0A099L0Q4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KGJ95682.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:KGJ95682.1};
GN   ORFNames=ND16A_1217 {ECO:0000313|EMBL:KGJ95682.1};
OS   Thalassotalea sp. ND16A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ95682.1, ECO:0000313|Proteomes:UP000029848};
RN   [1] {ECO:0000313|EMBL:KGJ95682.1, ECO:0000313|Proteomes:UP000029848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND16A {ECO:0000313|EMBL:KGJ95682.1,
RC   ECO:0000313|Proteomes:UP000029848};
RA   Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA   Hazen T.C.;
RT   "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT   Eastern Mediterranean Deep Water.";
RL   Submitted (AUG-2014) 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 FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:KGJ95682.1}.
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DR   EMBL; JQDZ01000068; KGJ95682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099L0Q4; -.
DR   STRING; 1535422.ND16A_1217; -.
DR   PATRIC; fig|1535422.3.peg.2206; -.
DR   eggNOG; COG0578; Bacteria.
DR   Proteomes; UP000029848; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KGJ95682.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029848}.
FT   DOMAIN          4..361
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   392 AA;  43755 MW;  4A0A91C2ED3D55BC CRC64;
     MKYDITIIGG GIAGAGVAQA ASAAGYKVLL LEQGEIAEQT SSCSSKLIHG GLRYLETGQL
     NLVFKALRER RALLRLAPDL VKPVAFYIPV YKNSRRGKWT LRAGLSLYAM LCILDPLSRF
     KQLPKSEWHK LEHLKHDNLQ AVFQYWDAQT DDAQLTRAVV NNAQQLGATI VTQAAFIDGT
     KTANGYAINY QLNNQFENQS NTNTVKVTTA FIVNAAGPWV NQVLKQITPS IPGFDIDWVQ
     GTHIILDTPA MTHVYYLESL IDDRVVFVMP WQGQTLVGTT ETLLANLPDE ITPKQQEIDY
     LLTIYQHYFP QRPVKVVDAF AGVRVLPKQQ QQAFDRKRQS IIYQGMTSPE VISLYGGKLT
     TFRATSKTVV ALIEKTLGKR KKIADVNTLT LD
//
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