ID Q8Z230_SALTI Unreviewed; 502 AA.
AC Q8Z230; A0A0C9CZ90; A0A0C9DUX7; Q7C5W7;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:CAD08095.1};
GN OrderedLocusNames=STY4277 {ECO:0000313|EMBL:CAD08095.1}, t3987
GN {ECO:0000313|EMBL:AAO71457.1};
GN ORFNames=CAJ76_01440 {ECO:0000313|EMBL:EDG8855621.1}, CAJ80_00960
GN {ECO:0000313|EMBL:EDG8900083.1}, CAJ85_00810
GN {ECO:0000313|EMBL:EDG8891066.1}, CAL67_00800
GN {ECO:0000313|EMBL:EDG8931297.1}, CB224_01160
GN {ECO:0000313|EMBL:EDH5799357.1}, CC884_02100
GN {ECO:0000313|EMBL:EDI0956654.1}, CC907_00805
GN {ECO:0000313|EMBL:EDI0992245.1}, CC972_01830
GN {ECO:0000313|EMBL:EDI1137482.1}, D4Z37_03895
GN {ECO:0000313|EMBL:EBS6525091.1}, D6Q30_03305
GN {ECO:0000313|EMBL:EBS1097412.1}, DKA88_00825
GN {ECO:0000313|EMBL:EBW2551187.1}, DNM71_01475
GN {ECO:0000313|EMBL:EBV0719042.1}, DNV09_00825
GN {ECO:0000313|EMBL:EBV1031322.1}, DS261_01475
GN {ECO:0000313|EMBL:EBX7032246.1}, DUQ91_01475
GN {ECO:0000313|EMBL:EBS0135634.1}, DUV11_01475
GN {ECO:0000313|EMBL:EBS5362818.1}, DVG36_00825
GN {ECO:0000313|EMBL:EBY2832315.1}, EBC38_01495
GN {ECO:0000313|EMBL:EBZ4080604.1}, EID90_00825
GN {ECO:0000313|EMBL:EBZ9853526.1}, ELQ62_00815
GN {ECO:0000313|EMBL:ECA4922587.1}, EU445_01460
GN {ECO:0000313|EMBL:ECB1383292.1}, EVI00_04045
GN {ECO:0000313|EMBL:ECB2191977.1}, F9R11_03985
GN {ECO:0000313|EMBL:EDB3134771.1}, F9Y21_03945
GN {ECO:0000313|EMBL:EDB3625388.1}, FI137_09500
GN {ECO:0000313|EMBL:EBG5394102.1}, G2227_03900
GN {ECO:0000313|EMBL:HAE0480072.1}, G2244_01460
GN {ECO:0000313|EMBL:HAE0415339.1}, G3982_000163
GN {ECO:0000313|EMBL:HAE3626682.1}, G3V49_000160
GN {ECO:0000313|EMBL:HAE1995308.1}, G4I71_001444
GN {ECO:0000313|EMBL:HAE6054254.1}, G4L28_000494
GN {ECO:0000313|EMBL:HAE6905981.1}, G4P30_000290
GN {ECO:0000313|EMBL:HAE7597027.1}, G4Y41_000187
GN {ECO:0000313|EMBL:HAE9013668.1}, G4Y55_000775
GN {ECO:0000313|EMBL:HAE9578096.1}, G9264_000160
GN {ECO:0000313|EMBL:HAF7396841.1}, G9C68_000648
GN {ECO:0000313|EMBL:HAF0685187.1}, GDI29_03985
GN {ECO:0000313|EMBL:EDH3994274.1}, GND71_000290
GN {ECO:0000313|EMBL:HAE7808581.1}, K3U68_19420
GN {ECO:0000313|EMBL:QZA28983.1}, ZZ17_00845
GN {ECO:0000313|EMBL:ECV8214333.1};
OS Salmonella typhi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370 {ECO:0000313|EMBL:CAD08095.1, ECO:0000313|Proteomes:UP000000541};
RN [1] {ECO:0000313|EMBL:CAD08095.1, ECO:0000313|Proteomes:UP000000541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18 {ECO:0000313|EMBL:CAD08095.1,
RC ECO:0000313|Proteomes:UP000000541};
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.,
RA Rutherford K., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2] {ECO:0000313|EMBL:AAO71457.1, ECO:0000313|Proteomes:UP000002670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2 {ECO:0000313|Proteomes:UP000002670}, and Ty2
RC {ECO:0000313|EMBL:AAO71457.1};
RX PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA Deng W., Liou S.R., Plunkett G.III., Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [3] {ECO:0000313|EMBL:HAE0415339.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=09-1703 {ECO:0000313|EMBL:HAE3626682.1}, 09-1978
RC {ECO:0000313|EMBL:HAE6054254.1}, 09-1979
RC {ECO:0000313|EMBL:HAE7597027.1}, 10-1436
RC {ECO:0000313|EMBL:HAE1995308.1}, 11-2088
RC {ECO:0000313|EMBL:HAE6905981.1}, 12-0098
RC {ECO:0000313|EMBL:HAF7396841.1}, 12-2005
RC {ECO:0000313|EMBL:HAE9013668.1}, 13-0747
RC {ECO:0000313|EMBL:HAF0685187.1}, 13-7562
RC {ECO:0000313|EMBL:HAE9578096.1}, IP E.88.374
RC {ECO:0000313|EMBL:HAE7808581.1},
RC Sam_1c96eabc-5ba9-4785-8bb4-b62bc64a6574
RC {ECO:0000313|EMBL:HAE0415339.1}, and
RC Sam_2e1fd039-ec06-4964-b74e-443d7665d7a0
RC {ECO:0000313|EMBL:HAE0480072.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [4] {ECO:0000313|EMBL:EBS0135634.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=116585 {ECO:0000313|EMBL:EDG8931297.1}, 132015
RC {ECO:0000313|EMBL:EDG8900083.1}, 14549
RC {ECO:0000313|EMBL:ECV8214333.1}, 186520
RC {ECO:0000313|EMBL:EDG8891066.1}, 189261
RC {ECO:0000313|EMBL:EDG8855621.1}, 257355
RC {ECO:0000313|EMBL:EBW2551187.1}, 338438
RC {ECO:0000313|EMBL:EDI1137482.1}, 339489
RC {ECO:0000313|EMBL:EDI0956654.1}, 348081
RC {ECO:0000313|EMBL:EDI0992245.1}, 365365
RC {ECO:0000313|EMBL:EDH5799357.1}, 524805
RC {ECO:0000313|EMBL:EBY2832315.1}, 531284
RC {ECO:0000313|EMBL:EBV1031322.1}, 539099
RC {ECO:0000313|EMBL:EBV0719042.1}, 550116
RC {ECO:0000313|EMBL:EBX7032246.1}, 550675
RC {ECO:0000313|EMBL:ECB1383292.1}, 550679
RC {ECO:0000313|EMBL:EBS5362818.1}, 568336
RC {ECO:0000313|EMBL:EBS0135634.1}, 588927
RC {ECO:0000313|EMBL:EBS6525091.1}, 606246
RC {ECO:0000313|EMBL:EBS1097412.1}, 619925
RC {ECO:0000313|EMBL:EBZ4080604.1}, 643219
RC {ECO:0000313|EMBL:EBZ9853526.1}, 656788
RC {ECO:0000313|EMBL:ECA4922587.1}, 673629
RC {ECO:0000313|EMBL:ECB2191977.1}, 731618
RC {ECO:0000313|EMBL:EBG5394102.1}, 814947
RC {ECO:0000313|EMBL:EDB3134771.1}, 815592
RC {ECO:0000313|EMBL:EDB3625388.1}, and 824494
RC {ECO:0000313|EMBL:EDH3994274.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAE0415339.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=09-1703 {ECO:0000313|EMBL:HAE3626682.1}, 09-1978
RC {ECO:0000313|EMBL:HAE6054254.1}, 09-1979
RC {ECO:0000313|EMBL:HAE7597027.1}, 10-1436
RC {ECO:0000313|EMBL:HAE1995308.1}, 11-2088
RC {ECO:0000313|EMBL:HAE6905981.1}, 12-0098
RC {ECO:0000313|EMBL:HAF7396841.1}, 12-2005
RC {ECO:0000313|EMBL:HAE9013668.1}, 13-0747
RC {ECO:0000313|EMBL:HAF0685187.1}, 13-7562
RC {ECO:0000313|EMBL:HAE9578096.1}, IP E.88.374
RC {ECO:0000313|EMBL:HAE7808581.1},
RC Sam_1c96eabc-5ba9-4785-8bb4-b62bc64a6574
RC {ECO:0000313|EMBL:HAE0415339.1}, and
RC Sam_2e1fd039-ec06-4964-b74e-443d7665d7a0
RC {ECO:0000313|EMBL:HAE0480072.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:QZA28983.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ISP2825 {ECO:0000313|EMBL:QZA28983.1};
RA Lee G.Y., Song J.;
RT "Complete Genome Sequence of Salmonella enterica Serovar Typhi Strain
RT ISP2825.";
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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DR EMBL; AE014613; AAO71457.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD08095.1; -; Genomic_DNA.
DR EMBL; AAFJDY010000012; EBG5394102.1; -; Genomic_DNA.
DR EMBL; AAGUIA010000001; EBS0135634.1; -; Genomic_DNA.
DR EMBL; AAGULE010000004; EBS1097412.1; -; Genomic_DNA.
DR EMBL; AAGVVD010000001; EBS5362818.1; -; Genomic_DNA.
DR EMBL; AAGWES010000003; EBS6525091.1; -; Genomic_DNA.
DR EMBL; AAHEBT010000001; EBV0719042.1; -; Genomic_DNA.
DR EMBL; AAHEEH010000001; EBV1031322.1; -; Genomic_DNA.
DR EMBL; AAHHUX010000001; EBW2551187.1; -; Genomic_DNA.
DR EMBL; AAHLZU010000001; EBX7032246.1; -; Genomic_DNA.
DR EMBL; AAHNRO010000001; EBY2832315.1; -; Genomic_DNA.
DR EMBL; AAHRAJ010000001; EBZ4080604.1; -; Genomic_DNA.
DR EMBL; AAHSWZ010000001; EBZ9853526.1; -; Genomic_DNA.
DR EMBL; AAHUNO010000001; ECA4922587.1; -; Genomic_DNA.
DR EMBL; AAHWPO010000001; ECB1383292.1; -; Genomic_DNA.
DR EMBL; AAHWWI010000002; ECB2191977.1; -; Genomic_DNA.
DR EMBL; AAKUKE010000001; ECV8214333.1; -; Genomic_DNA.
DR EMBL; AALNBT010000002; EDB3134771.1; -; Genomic_DNA.
DR EMBL; AALNGB010000002; EDB3625388.1; -; Genomic_DNA.
DR EMBL; AAMFQS010000001; EDG8855621.1; -; Genomic_DNA.
DR EMBL; AAMFQZ010000001; EDG8891066.1; -; Genomic_DNA.
DR EMBL; AAMFRD010000001; EDG8900083.1; -; Genomic_DNA.
DR EMBL; AAMFRJ010000001; EDG8931297.1; -; Genomic_DNA.
DR EMBL; AAMHNJ010000002; EDH3994274.1; -; Genomic_DNA.
DR EMBL; AAMICL010000001; EDH5799357.1; -; Genomic_DNA.
DR EMBL; AAMJUX010000002; EDI0956654.1; -; Genomic_DNA.
DR EMBL; AAMJVG010000001; EDI0992245.1; -; Genomic_DNA.
DR EMBL; AAMJWL010000001; EDI1137482.1; -; Genomic_DNA.
DR EMBL; DAAQQG010000001; HAE0415339.1; -; Genomic_DNA.
DR EMBL; DAAQQU010000002; HAE0480072.1; -; Genomic_DNA.
DR EMBL; DAARDQ010000001; HAE1995308.1; -; Genomic_DNA.
DR EMBL; DAARRK010000001; HAE3626682.1; -; Genomic_DNA.
DR EMBL; DAASLV010000011; HAE6054254.1; -; Genomic_DNA.
DR EMBL; DAASSY010000003; HAE6905981.1; -; Genomic_DNA.
DR EMBL; DAASYX010000001; HAE7597027.1; -; Genomic_DNA.
DR EMBL; DAATAS010000001; HAE7808581.1; -; Genomic_DNA.
DR EMBL; DAATOU010000001; HAE9013668.1; -; Genomic_DNA.
DR EMBL; DAATPQ010000002; HAE9578096.1; -; Genomic_DNA.
DR EMBL; DAATYW010000002; HAF0685187.1; -; Genomic_DNA.
DR EMBL; DAAWDS010000001; HAF7396841.1; -; Genomic_DNA.
DR EMBL; CP080960; QZA28983.1; -; Genomic_DNA.
DR RefSeq; NP_458385.1; NC_003198.1.
DR RefSeq; WP_000448178.1; NZ_WSUR01000001.1.
DR AlphaFoldDB; Q8Z230; -.
DR STRING; 220341.gene:17588108; -.
DR KEGG; stt:t3987; -.
DR KEGG; sty:STY4277; -.
DR PATRIC; fig|220341.7.peg.4370; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_0_6; -.
DR OMA; WAMAPHI; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.250.1890; -; 1.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 5..323
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 381..476
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 502 AA; 56907 MW; 31B93B1F5A333078 CRC64;
METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE
FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS
TGVRFGADSV LKPEIVRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATAARRENG
LWIVEAEDID TGKKYVWQAR GLVNATGPWV KQFFDEGMHL PSPYGIRLIK GSHIVVPRVH
NQKQAYILQN EDKRIVFVIP WMEEFSIIGT TDVEYKGDPK AVKIEESEIN YLLKVYNAHF
QKQLGRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK
LAEHAMEKLA SYYPGIGPAW TKTCVLPGGD IDGSREDYAA KLRRRYPFLT ESLARHYSRT
YGSNTEWILG EATSLLDLGE DFGHEFYEAE LKYLVDHEWV RRTEDAIWRR TKEGMWLTAE
QQSRITQWLA AYVEKHQLSL AS
//