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Multifunctional fusion protein [Includes: Glycerol-3-phosphate dehydrogenase [NAD(P) ] (EC 1.1.1.94) (NAD(P)H-dependent glycerol-3-phosphate dehydrogenase); Glycerol-3-phosphate acyltransferase (Acyl-PO4 G3P acyltransferase) (Acyl-phosphate--glycerol-3-phosphate acyltransferase) (G3P acyltransferase) (Lysophosphatidic acid synthase) (GPAT) (LPA synthase) (EC 2.3.1.n3)]

 J5W560_9FIRM            Unreviewed;       623 AA.
J5W560;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
12-SEP-2018, entry version 46.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|HAMAP-Rule:MF_01043};
Includes:
RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
AltName: Full=Lysophosphatidic acid synthase {ECO:0000256|HAMAP-Rule:MF_01043};
Short=GPAT {ECO:0000256|HAMAP-Rule:MF_01043};
Short=LPA synthase {ECO:0000256|HAMAP-Rule:MF_01043};
EC=2.3.1.n3 {ECO:0000256|HAMAP-Rule:MF_01043};
Includes:
RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
Name=plsY {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000313|EMBL:EJU19337.1};
Synonyms=gpsA {ECO:0000256|HAMAP-Rule:MF_00394};
ORFNames=HMPREF1152_0374 {ECO:0000313|EMBL:EJU19337.1};
Mogibacterium sp. CM50.
Bacteria; Firmicutes; Clostridia; Clostridiales;
Clostridiales Family XIII. Incertae Sedis; Mogibacterium.
NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU19337.1, ECO:0000313|Proteomes:UP000003142};
[1] {ECO:0000313|EMBL:EJU19337.1, ECO:0000313|Proteomes:UP000003142}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CM50 {ECO:0000313|EMBL:EJU19337.1,
ECO:0000313|Proteomes:UP000003142};
Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B.,
Sutton G., Nelson K.E.;
Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-
phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form
lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate
as fatty acyl donor, but not acyl-CoA or acyl-ACP.
{ECO:0000256|HAMAP-Rule:MF_01043}.
-!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1-
acyl-sn-glycerol 3-phosphate + phosphate. {ECO:0000256|HAMAP-
Rule:MF_01043}.
-!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) =
glycerone phosphate + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_00394,
ECO:0000256|RuleBase:RU000439, ECO:0000256|SAAS:SAAS00764424}.
-!- PATHWAY: Lipid metabolism; phospholipid metabolism.
{ECO:0000256|HAMAP-Rule:MF_01043}.
-!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
metabolism. {ECO:0000256|HAMAP-Rule:MF_00394,
ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764395}.
-!- SUBUNIT: Probably interacts with PlsX. {ECO:0000256|HAMAP-
Rule:MF_01043}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01043}; Multi-pass membrane protein {ECO:0000256|HAMAP-
Rule:MF_01043}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764434}.
-!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_00394,
ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00649394}.
-!- SIMILARITY: Belongs to the PlsY family. {ECO:0000256|HAMAP-
Rule:MF_01043}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01043}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJU19337.1}.
-----------------------------------------------------------------------
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EMBL; ALNL01000044; EJU19337.1; -; Genomic_DNA.
ProteinModelPortal; J5W560; -.
EnsemblBacteria; EJU19337; EJU19337; HMPREF1152_0374.
PATRIC; fig|936375.3.peg.1656; -.
OrthoDB; POG091H060E; -.
UniPathway; UPA00085; -.
UniPathway; UPA00940; -.
Proteomes; UP000003142; Unassembled WGS sequence.
GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 1.10.1040.10; -; 1.
HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
HAMAP; MF_01043; PlsY; 1.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR013328; 6PGD_dom2.
InterPro; IPR003811; G3P_acylTferase_PlsY.
InterPro; IPR006168; G3P_DH_NAD-dep.
InterPro; IPR006109; G3P_DH_NAD-dep_C.
InterPro; IPR011128; G3P_DH_NAD-dep_N.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02660; G3P_acyltransf; 1.
Pfam; PF07479; NAD_Gly3P_dh_C; 1.
Pfam; PF01210; NAD_Gly3P_dh_N; 1.
PRINTS; PR00077; GPDHDRGNASE.
SMART; SM01207; G3P_acyltransf; 1.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00023; TIGR00023; 1.
PROSITE; PS00957; NAD_G3PDH; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000313|EMBL:EJU19337.1};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01043};
Complete proteome {ECO:0000313|Proteomes:UP000003142};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
ECO:0000256|SAAS:SAAS00764341};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764418};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764418};
Membrane {ECO:0000256|HAMAP-Rule:MF_01043};
NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437,
ECO:0000256|SAAS:SAAS00764378};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00394,
ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00809767};
Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764418};
Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764418};
Reference proteome {ECO:0000313|Proteomes:UP000003142};
Transferase {ECO:0000313|EMBL:EJU19337.1};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01043};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01043}.
TRANSMEM 6 25 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 80 98 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
TRANSMEM 110 132 Helical. {ECO:0000256|HAMAP-
Rule:MF_01043}.
DOMAIN 296 450 NAD_Gly3P_dh_N.
{ECO:0000259|Pfam:PF01210}.
DOMAIN 470 610 NAD_Gly3P_dh_C.
{ECO:0000259|Pfam:PF07479}.
NP_BIND 301 306 NAD. {ECO:0000256|HAMAP-Rule:MF_00394}.
REGION 545 546 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00394}.
ACT_SITE 481 481 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00394}.
BINDING 399 399 NAD; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00394}.
BINDING 399 399 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00394}.
BINDING 430 430 NAD; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00394}.
BINDING 545 545 NAD. {ECO:0000256|HAMAP-Rule:MF_00394}.
BINDING 571 571 NAD. {ECO:0000256|HAMAP-Rule:MF_00394}.
SEQUENCE 623 AA; 67018 MW; DCBCDB50567FECA7 CRC64;
MNYVSLTIMV VIAYLIGNIS PATLIGRFYG IDIKKAGSGN AGTTNVLRVL GTKAAACTLV
IDILKGLVAV TIAQGRFNNL GAMLAFAAVV IGHIYPVIFK FKGGKGVATF IGAAMAINWP
STFAAALIAV IVAGVSKKMS LGSITAALMY PLLMLYYYPK DLPIAILMAL VILFTHRGNI
KRLMNGEEKE LSIGSRIREK LTAQSNTDTD ESFDAPGEES SMNIEKAHDN LDKFDKDEDM
VLTDSVHDDI LASGSRDELV NEATSINHTR VEVLDSAADY YKDVEIPQLK GSAKKKVAVI
GNGSFGTAIA NVIAHNGHRV TIYGRNKEDI NRIRETRVNE KYLPGAKLAD SIRFTSNLRT
GVSKRDIVIF AIPAQQFGRV IEKSAKYIDK EAILVNLAKG IENDSLKTMS QIAKSLVDNR
YVAVSGPSHA EEIVRNYPTT VVAASDDDDA AKEIQNILMS KTFRVYTGDD ILGVELGGAL
KNVIALGTGI ADGMKFGDNS KAALMTRGIH EISRLGEAMG AKSETFAGLS GIGDLMVTCS
SDLSRNRRCG LLIGGGMTPD EAVAEIKTTV EGFYTVEAAS RLAAKLGIEM PITDAVKSVI
DGNLKPRDAV ELLMNRDRKQ ENK


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