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Database: UniProt
Entry: A0A261GI58_9GAMM
LinkDB: A0A261GI58_9GAMM
Original site: A0A261GI58_9GAMM 
ID   A0A261GI58_9GAMM        Unreviewed;       587 AA.
AC   A0A261GI58;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BTA51_26515 {ECO:0000313|EMBL:OZG70396.1};
OS   Hahella sp. CCB-MM4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=1926491 {ECO:0000313|EMBL:OZG70396.1, ECO:0000313|Proteomes:UP000215632};
RN   [1] {ECO:0000313|EMBL:OZG70396.1, ECO:0000313|Proteomes:UP000215632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB-MM4 {ECO:0000313|EMBL:OZG70396.1,
RC   ECO:0000313|Proteomes:UP000215632};
RA   Sam K.-K., Lau N.-S., Dinesh B., Go F., Amirul A.-A.A.;
RT   "Genome sequence of Hahella sp. CCB-MM4 and discovery of its potential
RT   applications.";
RL   Submitted (DEC-2016) 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:OZG70396.1}.
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DR   EMBL; MRYI01000023; OZG70396.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261GI58; -.
DR   Proteomes; UP000215632; 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:InterPro.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
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; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
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   Pfam; PF16901; DAO_C; 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   Reference proteome {ECO:0000313|Proteomes:UP000215632}.
FT   DOMAIN          21..363
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          421..543
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   587 AA;  66203 MW;  487518F9612CA7CF CRC64;
     MEDLMRQPRA IESLIDGEAF DAIIIGGGIN GIGAYRELSL QGLKVLIVEK DDFCSKASSA
     LSRMIHGGLR YLENAEFELV RESLYERNRL LENAPHYVRP LETNIPLYSW TSGLFSAALR
     FLGINNKVTD RGALIVKLGL SLYDFFTRKD QQMPRHRLQG TRDTFQRWPS YSSSVKCSAV
     YYDAWISAPE RLAIELLQDG DQQQGKSHAL NYTLVESIDD DGVVVADTET GIRRRLRSRV
     IVNATGAWVD HCNRAAGINS RYLSGTKGSH IIVDHPELHR ELNGAMVYYE NSENRVCIMF
     PFLEKVLIGS TDIPVQEPGS ALCTEEEVDY ILASVKTIFP SIEIHKSDIC YRFSGVRPLV
     AASTETTGQI PRSHAIKVDQ IGTSGPRVYS LIGGKWTTFR ALAEQVTDQI LLDMDKIRIT
     STKTRKIGGG CHYPEDFNQL SRFLTEVSFK YSVPVSRVDI LLQRYGTTCL EILNHIRQAP
     DSALEYIPSY SRRELGYLIH REYVQTPLDL LQRRTTIAIE GLVTPLALAE ITGLMSKELH
     WDYGRTQAEY RAAAEYLNTH NGYQIDLDLP ETDGLADVFG DKHYVFN
//
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