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Database: UniProt
Entry: D4GQU6
LinkDB: D4GQU6
Original site: D4GQU6 
ID   GLPA2_HALVD             Reviewed;         563 AA.
AC   D4GQU6;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   10-APR-2019, entry version 53.
DE   RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A2;
DE            Short=G-3-P dehydrogenase A2;
DE            Short=G3PDH A2;
DE            EC=1.1.5.3;
GN   Name=gpdA2; OrderedLocusNames=HVO_A0269;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
OS   14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG   Plasmid pHV4.
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, AND DISRUPTION PHENOTYPE.
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. Functional analog of glpA1 required for the basal
CC       levels of glycerol-3-phosphate dehydrogenase activity, but not
CC       expressed during standard growth on glycerol or when glpA1 is
CC       knockout. {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   -!- 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   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {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; CP001955; ADE02027.1; -; Genomic_DNA.
DR   RefSeq; WP_013035148.1; NC_013966.1.
DR   ProteinModelPortal; D4GQU6; -.
DR   SMR; D4GQU6; -.
DR   STRING; 309800.C498_09986; -.
DR   EnsemblBacteria; ADE02027; ADE02027; HVO_A0269.
DR   GeneID; 8923720; -.
DR   KEGG; hvo:HVO_A0269; -.
DR   HOGENOM; HOG000004814; -.
DR   KO; K00111; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000008243; Plasmid pHV4.
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; Plasmid; Reference proteome.
FT   CHAIN         1    563       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit A2.
FT                                /FTId=PRO_0000428860.
FT   NP_BIND       4     32       FAD. {ECO:0000255}.
SQ   SEQUENCE   563 AA;  60955 MW;  50F390554781ED4C CRC64;
     MSYSVVVIGG GATGTGTARD LAMRGFDVTL VERGNLTEGT TGRTHGHLHS GARYAVSDKE
     SAVDCMRENR VLHRIAGHCI EDTGGLFVQL EGDSDDYFER KLAGCAECDI PTEVISGEEA
     RRREPYLTDA VERAIWVPDG AVDPFRLCVA NAASAVEHGA RIETHAEVVD LVVEGGRVAG
     VEVKRQGPNH HSEGAAGDTE TFEADYVVSA TGAWAGQLAA MAGVDLEMAI SKGAMVVTNV
     RQLDTVINRC LPKGEGDTII PHETTVLLGA NDDPVDDPDD YPEEQWEVDM MIDIASEMVP
     VVADARMIRA YWGVRPLYDP NPKSTTDPGD VTRNYFVLDH AERDGVAGFA SVVGGKLTTY
     REMAESVSDH VCEVLGVEEP CRTDEVPLPG SADPSALDEY MDEFDLRSPI ARRSGQRLGD
     RAPEVLDIDE PNPTLCECEA VTRAEVRDAI DQVGADLNGV RLRTRASMGN CQGGFCSHRL
     GAELYPDHGA EVARDAVDEL YQERWKGQRH ALWGEQLSQA MLNAMLHATT MNHDANHVAG
     DENIEYRAFD GGRTAVPEGS HGD
//
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