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Database: UniProt
Entry: A0A1C0AL27_9ACTN
LinkDB: A0A1C0AL27_9ACTN
Original site: A0A1C0AL27_9ACTN 
ID   A0A1C0AL27_9ACTN        Unreviewed;       525 AA.
AC   A0A1C0AL27;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A {ECO:0000313|EMBL:VEP40400.1};
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase, anaerobic, A subunit {ECO:0000313|EMBL:OCL33225.1};
GN   Name=glpA {ECO:0000313|EMBL:VEP40400.1};
GN   ORFNames=BCR15_05160 {ECO:0000313|EMBL:OCL33225.1}, TLA_TLA_01685
GN   {ECO:0000313|EMBL:VEP40400.1};
OS   Tessaracoccus lapidicaptus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1427523 {ECO:0000313|EMBL:OCL33225.1, ECO:0000313|Proteomes:UP000093501};
RN   [1] {ECO:0000313|Proteomes:UP000093501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IPBSL-7 {ECO:0000313|Proteomes:UP000093501};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OCL33225.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IPBSL-7 {ECO:0000313|EMBL:OCL33225.1};
RA   Puente-Sanchez F., Arce-Rodriguez A.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:VEP40400.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TLA_E {ECO:0000313|EMBL:VEP40400.1};
RA   Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA   Castillo E.;
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000516347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA   Castillo E.;
RL   Submitted (JAN-2019) 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}.
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DR   EMBL; MBQD01000022; OCL33225.1; -; Genomic_DNA.
DR   EMBL; LR214441; VEP40400.1; -; Genomic_DNA.
DR   RefSeq; WP_068751791.1; NZ_MBQD01000022.1.
DR   AlphaFoldDB; A0A1C0AL27; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000093501; Unassembled WGS sequence.
DR   Proteomes; UP000516347; 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; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093501}.
FT   DOMAIN          7..357
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   525 AA;  57507 MW;  18EFD6E6AC9EFA40 CRC64;
     MKRLDTDVVV IGGGSTGLGV VRDAAMRGYR AVLLERVDLG QGTTGRFHGL LHSGGRYVVS
     DPGSATECAE ENAILRRIQP GAIEDTGGFF VTLAGDDPAY ADKFLAGAAA TGVPATEISV
     KEALRREPRL DPHIQRAIEV ADGSVDGWQL VWGAARSAME HRAKILTYHR VTKIERDGDR
     VAAVLCRDEK GGEDVRIDCT FVLNCAGPWA GQIAEMAGAS PVEVVPGRGI MIAMNHRLVN
     TVINRCVYPT DGDILVPVHT VSIIGTTDVH ETDPDHLPIP RNEVQQMLDA GEAMIPGFRK
     ARALHAWSGS RPLIKDKRVS VEDTRHMSRG MAVIDHSKRD GLLGMLTIGG GKLTTYRLMA
     EHIVDAMNEQ LGEDRPCTTA DEVVPGSRDG RLYTVTHRLE DREEDRLDDP IICECELMNR
     SMFVKALHEQ PDATLDDLRR QLRLGMGPCQ GGFCAARAAG LACSEQVADA ERASGLLRLF
     LKHRWIGLWP ILYGQQVRQT ALDHWIFAGT LDVEHLPQPE EEIVR
//
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