ID   E4NLP9_HALBP            Unreviewed;       407 AA.
AC   E4NLP9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ADQ67252.1};
GN   OrderedLocusNames=Hbor_16840 {ECO:0000313|EMBL:ADQ67252.1};
GN   ORFNames=C499_14455 {ECO:0000313|EMBL:ELY25027.1};
OS   Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS   KCTC 4070 / PR3).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halogeometricum.
OX   NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ67252.1, ECO:0000313|Proteomes:UP000006663};
RN   [1] {ECO:0000313|EMBL:ADQ67252.1, ECO:0000313|Proteomes:UP000006663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC   {ECO:0000313|Proteomes:UP000006663}, and PR 3
RC   {ECO:0000313|EMBL:ADQ67252.1};
RX   PubMed=21304651; DOI=10.4056/sigs.23264;
RA   Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA   Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Halogeometricum borinquense type strain
RT   (PR3).";
RL   Stand. Genomic Sci. 1:150-159(2009).
RN   [2] {ECO:0000313|EMBL:ELY25027.1, ECO:0000313|Proteomes:UP000011585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY25027.1,
RC   ECO:0000313|Proteomes:UP000011585};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001690; ADQ67252.1; -; Genomic_DNA.
DR   EMBL; AOHT01000045; ELY25027.1; -; Genomic_DNA.
DR   RefSeq; WP_006056194.1; NZ_AOHT01000045.1.
DR   AlphaFoldDB; E4NLP9; -.
DR   STRING; 469382.Hbor_16840; -.
DR   GeneID; 9993503; -.
DR   KEGG; hbo:Hbor_16840; -.
DR   PATRIC; fig|469382.19.peg.2850; -.
DR   eggNOG; arCOG00753; Archaea.
DR   HOGENOM; CLU_015740_0_1_2; -.
DR   OrthoDB; 36306at2157; -.
DR   Proteomes; UP000006663; Chromosome.
DR   Proteomes; UP000011585; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985:SF36; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 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:UP000006663}.
FT   DOMAIN          6..350
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   407 AA;  43000 MW;  E3E8E8FDA90B3F96 CRC64;
     MADDTDVVVI GGGATGAGIV RDLALRGVDV TLVERGGLSA GTSGRSHGLL HSGARYAEAD
     EVGARECIAE NRILRDIAGE CVRDTGGLFL QLAEDDPEYF EAKRTACEDI GIPIETLSGD
     EVRNEISGLS EAVERAMKVP DAVVSPSRLV AANAADARDH GATILTNAPV EDLHVEDGRI
     TGVKVGGSVG ETIAAKQVVN AAGAWAEDVG RMAGVEVAMR PTKGVMVSVQ YDGLGPVLNR
     ARDPADGDIV VPHDGEVVLG TTSIEVDDPD DYPEDAQEVE RMVEECSKML PPAREAERVR
     TWWGVRPLYA PDEDSREGAR GISRGFFCVD HGDDGVENFT SIVGGKLTTY RQMAEATTDR
     VCEKLGVAAD CRTAAKRLPG ADDPEQLDAY VTEFGGAGPT DEDVVRG
//