GLPA1_HALVD
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 03-AUG-2022, entry version 62.
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 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
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, DISRUPTION PHENOTYPE, ACTIVITY REGULATION,
RP 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 metabolism.
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 -!- ACTIVITY REGULATION: Up-regulated by glycerol and no inhibition by
CC glucose. {ECO:0000269|PubMed:21725010}.
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 -!- INDUCTION: Up-regulated by glycerol 3-phosphate.
CC {ECO:0000269|PubMed:21725010}.
CC -!- DISRUPTION PHENOTYPE: Unable to grow on glycerol. Can be complemented
CC in trans by glpA2 under the control from a strong promoter.
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; CP001956; ADE05130.1; -; Genomic_DNA.
DR RefSeq; WP_013035654.1; NC_013967.1.
DR AlphaFoldDB; D4GYI2; -.
DR SMR; 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 HOGENOM; CLU_015740_0_1_2; -.
DR OMA; GVMTIMN; -.
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; 1.10.10.1100; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
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 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; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..586
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT A1"
FT /id="PRO_0000428859"
FT REGION 559..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
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
