ID M6HY77_LEPIR Unreviewed; 669 AA.
AC M6HY77;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase (NAD(+)) {ECO:0000313|EMBL:EMM95851.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:EMM95851.1};
GN ORFNames=LEP1GSC158_0392 {ECO:0000313|EMBL:EMM95851.1};
OS Leptospira interrogans serovar Zanoni str. LT2156.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1001601 {ECO:0000313|EMBL:EMM95851.1, ECO:0000313|Proteomes:UP000012089};
RN [1] {ECO:0000313|EMBL:EMM95851.1, ECO:0000313|Proteomes:UP000012089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2156 {ECO:0000313|EMBL:EMM95851.1,
RC ECO:0000313|Proteomes:UP000012089};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., 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:EMM95851.1}.
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DR EMBL; AFMF02000027; EMM95851.1; -; Genomic_DNA.
DR AlphaFoldDB; M6HY77; -.
DR Proteomes; UP000012089; 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; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.40.1130.10; Glycerol-3-phosphate (1)-acyltransferase; 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; 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 109..243
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 669 AA; 75134 MW; 2481FCB821D7D991 CRC64;
MVEKESSVGK WQKEFFENIH LFKRSGMTED EAKKILQKFL YLSSVTPMPP VMEVFKEPNL
LESVGVYTSP EQRSREFMME FLSPIMKQFT VEGVENLKAV KPLIGKYPVT LISNHLSHLD
APAIFHQLYN CSPEGKSIAE QLVFIAGRLA YEPDFTRLGL YMFGTLLVCS KRDMADNPSL
SDLMTKINMR AFRHSQKLQS EGKIVAIFPE GTRSRDGRLM PFVETVYHYV ANKVIIPISL
EKTDKILPTT SLLFNQVNGK LVIGKPVLVG ELSRKQMDSF PKEVEQLQFP EHGDKKQFLI
DNLALLVGSN LNKHQHGTYR NLYKGDVPGK NILIKIPKEP EEKIVVIGAS SMSIAVATLL
ANKDVLVYLY HPDQTYTEQC NTERRELKYY PLYKLPPNLV FTSDVEVLKT ATLFIQGTNP
WELINVYPEI QPYLNRNKAP FFNVVKGFTS TGLILDEVQN AFGLEDDRLG VIAGACYPDQ
IMERKISGFE IAASNATLIP RVQKLFTTGY IFPRPARIPT DVKGVQLGGA LKTIYALAMG
IVEGYFTQTL GGNVDNSLFH LSNRFFTEMT TIGTKMGGQP ETFLGLSGLT DFMLSCFGTD
AKDRKTGYDI AYGSSSEKMS NGFYGLKVMP NLMKISAETP VLSAAYEIVI NKKDVNQIIE
MLEGRLARV
//
