ID A4MWY8_HAEIF Unreviewed; 334 AA.
AC A4MWY8;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:EDJ89807.1};
DE EC=2.3.1.15 {ECO:0000313|EMBL:EDJ89807.1};
GN ORFNames=CGSHi22121_05010 {ECO:0000313|EMBL:EDJ89807.1};
OS Haemophilus influenzae 22.1-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374927 {ECO:0000313|EMBL:EDJ89807.1, ECO:0000313|Proteomes:UP000004131};
RN [1] {ECO:0000313|EMBL:EDJ89807.1, ECO:0000313|Proteomes:UP000004131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.1-21 {ECO:0000313|EMBL:EDJ89807.1,
RC ECO:0000313|Proteomes:UP000004131};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; AAZD01000001; EDJ89807.1; -; Genomic_DNA.
DR AlphaFoldDB; A4MWY8; -.
DR Proteomes; UP000004131; Unassembled WGS sequence.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF9; TYPE II NADH:QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EDJ89807.1};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transferase {ECO:0000313|EMBL:EDJ89807.1}.
FT DOMAIN 3..321
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 334 AA; 36983 MW; E4387694F5CF81DF CRC64;
MKNVVIVGGG AGGIELATFL GNKLGRQKQA KVTLVDRNAT HLWKPLLHEI ATGVMDDGID
SLSYRAHGKN HFFSFEQGSI IRINREQKYV ELAPVYGQEG DMLVIARRIP YDYLVIAIGS
KSNDFNTKGV ADNCIFLDSS KQALRFQHKL LELFLKFSEN RALDDIGEEE FKQKLVDENK
VNIAIVGGGA TGVELTAELY HAAEDLSSYG YGKIDSSCLQ VTLVEAGTRL LPALPENLSA
AVLDELKEMG ANVQLNTMIT EAQPNTLITK DGREIKADLI VWAAGVRVST VTQQFDGLEI
NRINQLVVKD TLQTTVDDSI FCDWRLCCIY TIKW
//
