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Database: UniProt
Entry: D4GYI2
LinkDB: D4GYI2
Original site: D4GYI2 
ID   GLPA1_HALVD             Reviewed;         586 AA.
AC   D4GYI2;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   10-APR-2019, entry version 49.
DE   RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A1;
DE            Short=G-3-P dehydrogenase A1;
DE            Short=G3PDH A1;
DE            EC=1.1.5.3;
GN   Name=gpdA1; OrderedLocusNames=HVO_1538;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
OS   14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
RA   Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
RA   Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
RA   Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, ACTIVITY
RP   REGULATION, AND INDUCTION BY GLYCEROL 3-PHOSPHATE.
RC   STRAIN=DS2 / DS70;
RX   PubMed=21725010; DOI=10.1128/JB.00276-11;
RA   Rawls K.S., Martin J.H., Maupin-Furlow J.A.;
RT   "Activity and transcriptional regulation of bacterial protein-like
RT   glycerol-3-phosphate dehydrogenase of the haloarchaea in Haloferax
RT   volcanii.";
RL   J. Bacteriol. 193:4469-4476(2011).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone
CC       phosphate. Required for growth on glycerol and for glycerol
CC       metabolism. {ECO:0000269|PubMed:21725010}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000269|PubMed:21725010};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Up-regulated by glycerol and no inhibition by
CC       glucose. {ECO:0000269|PubMed:21725010}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane
CC       bound GlpC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by glycerol 3-phosphate.
CC       {ECO:0000269|PubMed:21725010}.
CC   -!- DISRUPTION PHENOTYPE: Unable to grow on glycerol. Can be
CC       complemented in trans by glpA2 under the control from a strong
CC       promoter. {ECO:0000269|PubMed:21725010}.
CC   -!- MISCELLANEOUS: H.volcanii contains 2 glpABC operons, one located
CC       on the main chromosome and the other on megaplasmid pHV4.
CC       {ECO:0000305|PubMed:21725010}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; CP001956; ADE05130.1; -; Genomic_DNA.
DR   RefSeq; WP_013035654.1; NC_013967.1.
DR   ProteinModelPortal; D4GYI2; -.
DR   STRING; 309800.C498_03045; -.
DR   EnsemblBacteria; ADE05130; ADE05130; HVO_1538.
DR   GeneID; 8925946; -.
DR   KEGG; hvo:HVO_1538; -.
DR   eggNOG; arCOG00753; Archaea.
DR   eggNOG; arCOG05746; Archaea.
DR   eggNOG; COG0578; LUCA.
DR   HOGENOM; HOG000004814; -.
DR   KO; K00111; -.
DR   OMA; IRSFWGV; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   InterPro; IPR017752; G3P_DH_GlpA_su.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR03377; glycerol3P_GlpA; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    586       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit A1.
FT                                /FTId=PRO_0000428859.
FT   NP_BIND       6     34       FAD. {ECO:0000255}.
FT   COMPBIAS    537    585       Asp-rich.
SQ   SEQUENCE   586 AA;  63487 MW;  451BB4B96EC64127 CRC64;
     MKKSPSVLVI GGGSTGTGIA RDLAMRGLDV TLVEKGNLTH GTTGRMHGLL HSGGRYAVSD
     QPSAKECIEE NRVLRRIAGH CVEMTGGLFV QRPEDSDEYF EKKLEGCREC GIPAEVLSAE
     EAREIEPYLA KDIKRAIKVP DGAVDPFRLC VANAASAVEH GARIETHSEV TDVLVEGGEV
     VGVEVTHQTG TGPYVHGEPG EVEEIRADYV VNATGAWAGQ IGDFAGVNVE VRPSKGVMTI
     MNTRQVDTVV NRCRPKGDAD IIVPHETTCI LGTTDEEVED PEDYPEEGWE VDLMIETLSE
     LVPMLADART IRSFWGVRPL YEPPGTGTED PTDITREFFL LDHADRDDLP GMTSIVGGKL
     TTYRMMAEQI SDHVCEKLGV DAECRTADEP LPGSEDFTVL RDYMDDFGLR SPIGRRSAQR
     LGSRADEVLN SVDPNPVVCE CEAVTRAEIQ DALDTAGTDL NSVRIQTRAS MGNCQGAICC
     HRMANELAPE YDEKTVRASL DDLYQERWKG ERHAMWGTQL SQTALKHMLH AATMNRDEDP
     AAADADIDFA AFDDGVASGG AVADGGRERA ADRADDDALG GADGDN
//
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