ID Q2SEM4_HAHCH Unreviewed; 536 AA.
AC Q2SEM4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ABC30900.1};
GN OrderedLocusNames=HCH_04193 {ECO:0000313|EMBL:ABC30900.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC30900.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC30900.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC30900.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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}.
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DR EMBL; CP000155; ABC30900.1; -; Genomic_DNA.
DR RefSeq; WP_011397967.1; NC_007645.1.
DR AlphaFoldDB; Q2SEM4; -.
DR STRING; 349521.HCH_04193; -.
DR KEGG; hch:HCH_04193; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_6; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000000238; Chromosome.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000000238}.
FT DOMAIN 17..338
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 430..506
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 536 AA; 61011 MW; 15BF315D89C5A9E3 CRC64;
MQLRDNNLSK VRRLSFDALV IGGGINGAVS AAAMSARGLK VALIDRGDFA GSTSQESSNL
AWGGIKYMET YEFGLVRKLC MSRNKLMRSY PSTVQEIRFF TTIKKGFRYP PWFLYLGGVL
YWFMGNGFTR FPHYLTPERI SREEPIVNTE GSTGGFEYSD AFLHDNDARF VFNFIRRAMD
YGCIAANYVE SVSAHWADRI WTINARDNIS GEEFQIRAGL LINACGPFVD DHNRLTGQTT
KYRHAFSKGI HLIVDRITQN KRVLTFFADD GRLFFVIPMG PKTCIGTTDT RMESPIATVT
PEDRKFVLDN INARLRLPQP LTESDVVAER CGVRPLAVQG DNGAKTDWLQ LSRKHVIEVD
AETRHISIFG GKLTDCLNVG DEICQAAAEL GLYPPYPNTI WYGEPPNRVK EEFMHQARLM
DLDSLTPPSS SEKLSIRLWR RYAAHAFDLL ETIRADPRQA ELLIENAEYL RCEIEQAARR
EMVTKLDDFL RRRSKISLVV RRDKIKSAQG LREACRILFG DEADEKWAEY FKETSA
//
