ID A0A200HKR2_9ACTN Unreviewed; 575 AA.
AC A0A200HKR2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:OUZ12815.1};
GN ORFNames=BHE97_00990 {ECO:0000313|EMBL:OUZ12815.1};
OS Aeromicrobium sp. PE09-221.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1898043 {ECO:0000313|EMBL:OUZ12815.1, ECO:0000313|Proteomes:UP000195423};
RN [1] {ECO:0000313|EMBL:OUZ12815.1, ECO:0000313|Proteomes:UP000195423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE09-221 {ECO:0000313|EMBL:OUZ12815.1,
RC ECO:0000313|Proteomes:UP000195423};
RX PubMed=28218694;
RA Matobole R.M., van Zyl L.J., Parker-Nance S., Davies-Coleman M.T.,
RA Trindade M.;
RT "Antibacterial Activities of Bacteria Isolated from the Marine Sponges
RT Isodictya compressa and Higginsia bidentifera Collected from Algoa Bay,
RT South Africa.";
RL Mar. Drugs 15:E47-E47(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUZ12815.1}.
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DR EMBL; MIJB01000002; OUZ12815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200HKR2; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000195423; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; 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:UP000195423}.
FT DOMAIN 24..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 408..533
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 545..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 62881 MW; 429E457D7C730B30 CRC64;
MRSVALSPQQ RRDAIRAMAE EPLDVLVIGG GVVGGGAALD AATRGLSVGL VEARDFASGT
SSRSSKLIHG GLRYLEMLDF RLVAEALAER GLLIERLAPH LVKPVPFIYP LTHHVWERVY
AGTGVLMYDS MAALSGRSRG VPHHTHLTRR GARKRMPALR KDALVGALHY YDGQVDDARH
TMFLSRTAAA YGAHVASRTR VVDLVREGDR VVGAHIKDLE SGETHEARAK QIINATGVWT
DETQGMAGER GQFHVRASKG IHLVVPRDRI RGESGLILRT ETSVLFVIPW GRHWIIGTTD
TDWDLSKDHP AASAKDIDYL LEHVNRVLVE PLTHDDVEGV YAGLRPLLAG ESDATSKLSR
EHAVSTATKG LVVIAGGKYT TYRVMAKDAV DAAVDAMAVQ LDRKVPASCT EDVPLLGADG
YEAMWNQRTA LAARHGIGVG RIEHLLNRYG SLTLEVLDLI AERPDLGQAL TGGDDYLRAE
VVYGVTHEGA RHLDDIIARR TRLSIETFDR GTGVAEEVAE LMGEELGWSA EQREREVDHY
VKRVEAERES QTMPDDETAD AARKGAPDVV PVVER
//
