ID M6U7M7_9LEPT Unreviewed; 809 AA.
AC M6U7M7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase (NAD(+)) {ECO:0000313|EMBL:EMO41002.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:EMO41002.1};
GN ORFNames=LEP1GSC186_4419 {ECO:0000313|EMBL:EMO41002.1};
OS Leptospira noguchii serovar Autumnalis str. ZUN142.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1085540 {ECO:0000313|EMBL:EMO41002.1, ECO:0000313|Proteomes:UP000012153};
RN [1] {ECO:0000313|EMBL:EMO41002.1, ECO:0000313|Proteomes:UP000012153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZUN142 {ECO:0000313|EMBL:EMO41002.1,
RC ECO:0000313|Proteomes:UP000012153};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Matthias M.A., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|RuleBase:RU000437}.
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:EMO41002.1}.
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DR EMBL; AHOP02000025; EMO41002.1; -; Genomic_DNA.
DR RefSeq; WP_004438259.1; NZ_AHOP02000025.1.
DR AlphaFoldDB; M6U7M7; -.
DR Proteomes; UP000012153; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NAD {ECO:0000256|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264}.
FT DOMAIN 530..657
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 809 AA; 90782 MW; F286978FEDA01EA6 CRC64;
MEEIKSSVIV PENIAVLGGG PMGIYLSTYL SPKAKEIYLW YDDRKKAAKI EKERIASLLE
DSISVPENVR IKSEFDFLKN GSWVIIIAVP SRLMEGILDE LSKVLDKHSS HFIFTFTKGL
LSTSTRKKTK CITYSEYLQK LSAAGGFKDV EYTAVNGPNL LGELKRGHHS FYSLASSGTK
SIEIFETLFC GSGNHTKTYE DLTGLEVFGA MKNPIAIACG IASGIPECGS NFEGELISLG
YSEITTFLKA LEIPTQLVQE YGLADLIASC TSRYSRNKAY GHRFVHKLIS GEDHPNLIER
IELFFNPAEF IQKEVSQSES HVEGAFALAS IISLAEEKNI EIPLYDTLFQ ILTRRVSPTE
LIRFVSKSTS DEVRHISKTA TKRSGLGMAS GKKFQEALSK NVQRRINGQP GMTDRILKQS
SLLIKSLEKR YQEAKGSNDA TDLLQIPKEI QLWNEVEKKF QETGNKDLTR ILDFYVTEIA
DDYKPFLRDA LIHLIAPTRY VLSGFKSGAG LPKIGGCIKE VKALASRYDI LYTPTHRSHL
DSIEVAFGLK WLGLPVPRYA ADKKVMATPG LASVLKSLGA YMVDRKRNRN ILYLECLTQY
STMMLEAGIP TLVYPEGTRS RTGGILPIKT GILSTSVEAY KHTGSEVIVV PIVLSYENVP
EDEEFCGKDK KPGFKDFFYK RKEVYMDLCE PIPVSRYIHE EDPTGSIGFE ITQGWKKYRR
ILPNQLVARM IVETGGEVST NELKNLIKET LLTKKGNYLI QDSNEILKRG LKILKQRKII
FLDNENIKVL DKGLIQYYAN MCSDESSYS
//
