ID V2Q9Q5_9BACT Unreviewed; 534 AA.
AC V2Q9Q5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A {ECO:0000313|EMBL:USF23383.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:USF23383.1};
DE SubName: Full=Glycerol-3-phosphate dehydrogenase, anaerobic, A subunit {ECO:0000313|EMBL:ESJ97701.1};
GN Name=glpA {ECO:0000313|EMBL:USF23383.1};
GN ORFNames=N508_000441 {ECO:0000313|EMBL:USF23383.1}, N508_01626
GN {ECO:0000313|EMBL:ESJ97701.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ97701.1};
RN [1] {ECO:0000313|EMBL:ESJ97701.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ97701.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF23383.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23383.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF23383.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23383.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYGZ01000018; ESJ97701.1; -; Genomic_DNA.
DR EMBL; CP097562; USF23383.1; -; Genomic_DNA.
DR RefSeq; WP_023276450.1; NZ_FTRD01000001.1.
DR AlphaFoldDB; V2Q9Q5; -.
DR STRING; 1379858.N508_01626; -.
DR GeneID; 78587183; -.
DR PATRIC; fig|1379858.3.peg.1626; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_0_1_0; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000017429; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; 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 PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:USF23383.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017429}.
FT DOMAIN 6..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 534 AA; 58748 MW; E8258AE4B7605679 CRC64;
MISTTVIIIG GGATGSGVLR DLSMRGIPAI MLEQGGLAYG TSSRFHGLLH SGARYAVNDN
ESAKECIEEN MILRKIGKHC VELTEGFFVQ TPEDDKEFAP KWLEGCKSAG IKTEEISLEE
AFKLEPNLSR DISKVYKVPD SCIDGFRLVW QNAMSARKYG GDLYTYHKVI EIITESGKVK
GVKALNKVTN EVVEFGCDYI VNASGSWAGE MVALSGLAPL PISPDRGTLI VFNHRFTSRV
INRLHKSSDG DIFVPHGSVT ILGTTSAEAN APDDKTPTSQ EVKKLLDIGR VVFPYVDDYR
ILRAFAGTRP LYGAKGAGRS ASRNFNIVNH TEEGLSGFVS IFGGKLTTYR LMAEKVSDVV
ADMAGVTAKC RTADEPIIQD VSEHTISKAK KYFPQGAVNI VVDRIGADFE EVLNNIENSN
EKNELICECE MVTLSEIKYV AKDAASYYLN DIRLRTRLGM GTCQGTFCSL RAIAALENEN
IEMKLKPSDN IKNFLQERWN GLRPALWGGQ LREAELTRAI YLSTLNFDGE SYEA
//