GLPA_HAEIN
ID GLPA_HAEIN Reviewed; 563 AA.
AC P43799;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A;
DE Short=G-3-P dehydrogenase;
DE EC=1.1.5.3;
GN Name=glpA; OrderedLocusNames=HI_0685;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 -!- 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 inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Loosely bound to the cytoplasmic
CC membrane often occurring in vesicles associated with fumarate
CC reductase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; L42023; AAC22345.1; -; Genomic_DNA.
DR PIR; E64086; E64086.
DR RefSeq; NP_438845.1; NC_000907.1.
DR RefSeq; WP_005694610.1; NC_000907.1.
DR AlphaFoldDB; P43799; -.
DR SMR; P43799; -.
DR STRING; 71421.HI_0685; -.
DR EnsemblBacteria; AAC22345; AAC22345; HI_0685.
DR KEGG; hin:HI_0685; -.
DR PATRIC; fig|71421.8.peg.716; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_0_1_6; -.
DR OMA; GVMTIMN; -.
DR PhylomeDB; P43799; -.
DR BioCyc; HINF71421:G1GJ1-720-MON; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000000579; 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:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
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:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.1100; -; 1.
DR Gene3D; 3.50.50.60; -; 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 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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..563
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT A"
FT /id="PRO_0000126095"
FT BINDING 20..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 563 AA; 61920 MW; 7E662A80F4E1EED6 CRC64;
MGLSPSIYKD VGDLSSLSTD VIIIGGGATG AGIARDCALR GIDCILLERR DIATGATGRN
HGLLHSGARY AVNDQESAEE CIKENRILRK IARHCVDETE GLFITLPEDS LDYQKTFLES
CAKSGIDAQA IDPELAKIME PSVNPDLVGA VVVPDGSIDP FRLTASNMMD ATENGAKMFT
YCEVKNLIRE GGKVIGVNAY DHKNRRERQF FAPLVVNAGG IWGQGIAEYA DLKIKMFPAK
GALLVMGHRI NKLVINRCRK PADADILVPG DTICVIGTTS SRIPYDQIDN MEVTPEEVDI
LFREGEKLAP SLRHTRVLRA YAGVRPLVAS DDDPSGRNVS RGIVLLDHAE RDGLDGFITI
TGGKLMTYRL MAEWATDLVC KKLNKTARCV TAEQPLPGST ESRQETNQKV ISLPSTIRYS
AVYRHGSRAT RLLEKERLDR SMVCECEAVT AGEVRYAVDE LDVNNLVDLR RRSRVGMGTC
QAELCACRAA GLMNRFEVAT PRQSTTQLSA FMEERWRGIE PIAWGEAIRE AEFTSWMYAS
VLGLNDVKPL DEQAQQGTDS NEF
