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Database: UniProt
Entry: P43799
LinkDB: P43799
Original site: P43799 
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   10-APR-2019, entry version 123.
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.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   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,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         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
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 inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Loosely bound to
CC       the cytoplasmic membrane often occurring in vesicles associated
CC       with fumarate reductase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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   ProteinModelPortal; P43799; -.
DR   SMR; P43799; -.
DR   STRING; 71421.HI_0685; -.
DR   EnsemblBacteria; AAC22345; AAC22345; HI_0685.
DR   GeneID; 949605; -.
DR   KEGG; hin:HI0685; -.
DR   PATRIC; fig|71421.8.peg.716; -.
DR   eggNOG; ENOG4107R5Y; Bacteria.
DR   eggNOG; COG0578; LUCA.
DR   KO; K00111; -.
DR   OMA; IRSFWGV; -.
DR   PhylomeDB; P43799; -.
DR   BioCyc; HINF71421:G1GJ1-720-MONOMER; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IBA:GO_Central.
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:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] 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; 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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; FAD;
KW   Flavoprotein; Membrane; Oxidoreductase; Reference proteome.
FT   CHAIN         1    563       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit A.
FT                                /FTId=PRO_0000126095.
FT   NP_BIND      20     48       FAD. {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
//
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