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 27-MAR-2024, entry version 69.
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 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC 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 / VKM
RC 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., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., 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 levels of
CC glycerol-3-phosphate dehydrogenase activity, but not expressed during
CC standard growth on glycerol or when glpA1 is knockout.
CC {ECO:0000269|PubMed:21725010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, 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 kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC GlpC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:21725010}.
CC -!- MISCELLANEOUS: H.volcanii contains 2 glpABC operons, one located on the
CC 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}.
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DR EMBL; CP001955; ADE02027.1; -; Genomic_DNA.
DR RefSeq; WP_013035148.1; NC_013966.1.
DR AlphaFoldDB; D4GQU6; -.
DR SMR; D4GQU6; -.
DR PaxDb; 309800-C498_09986; -.
DR EnsemblBacteria; ADE02027; ADE02027; HVO_A0269.
DR GeneID; 8923720; -.
DR KEGG; hvo:HVO_A0269; -.
DR eggNOG; arCOG00753; Archaea.
DR eggNOG; arCOG05746; Archaea.
DR HOGENOM; CLU_015740_0_1_2; -.
DR OrthoDB; 36306at2157; -.
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:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) 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 CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
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 NCBIfam; TIGR03377; glycerol3P_GlpA; 1.
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 Pfam; PF04324; Fer2_BFD; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; FAD; Flavoprotein; Membrane; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..563
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT A2"
FT /id="PRO_0000428860"
FT BINDING 4..32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="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
//
