ID A0A1Y6IVM0_9VIBR Unreviewed; 547 AA.
AC A0A1Y6IVM0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN Name=glpA {ECO:0000313|EMBL:SMS01699.1};
GN ORFNames=VIM7927_03003 {ECO:0000313|EMBL:SMS01699.1};
OS Vibrio mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=474394 {ECO:0000313|EMBL:SMS01699.1, ECO:0000313|Proteomes:UP000196125};
RN [1] {ECO:0000313|EMBL:SMS01699.1, ECO:0000313|Proteomes:UP000196125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7927 {ECO:0000313|EMBL:SMS01699.1,
RC ECO:0000313|Proteomes:UP000196125};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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|ARBA:ARBA00000153};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005157}.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC GlpC. {ECO:0000256|ARBA:ARBA00011331}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR EMBL; FXXI01000006; SMS01699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6IVM0; -.
DR OrthoDB; 9801699at2; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000196125; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 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 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 Pfam; PF04324; Fer2_BFD; 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; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SMS01699.1}.
FT DOMAIN 10..359
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 431..483
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 547 AA; 60048 MW; A3D193048CA779AD CRC64;
MTFAQRLETD VVIIGGGATG TGIMRDCALR GIGCILLERD DIASGTTGRN HGLLHSGARY
AVTDPESAKE CIRENQILRR VARHCVEPTD GLFITLPEDD LSYQDEFIHA CGVAGIEATR
LSAREALALE PHVNPQLTGA VKVPDGTLDP FRLCTANVLD AKEHGARLLN RTLVLGLIRQ
GDTVLGVHAL RTTTGEHLDI YAREVINAAG IWGQNICEYA DLNIRMFPAK GSLLILDYRI
NNLVINRCRK PSDADILVPG DTISLIGTTS EHVDYAQIDN LQVTEHEVDL LLREGEKLAP
IMANTRVLRA YAGVRPLVSV DDDGSGRNIS RGIVLLDHEK RDGLKGLTTI TGGKLMTYRL
MAEWATDTVA RKLGNEKPCE THTQPLPGAN DVPKAVRKTA SIAKPVYESA IYRHGERAGQ
FLADNPESQS IVCECEMVTA GEIEYAIKQL DVKNLIDLRR RTRLGMGPCQ GELCSYRAAA
LFSEYAGMDG CESSSLLTDF LEERWKGIKP IFWGDALREA EFSYWIYQGL LGAGDIPANQ
SRQEDNE
//
