PGPS1_CHICK
ID PGPS1_CHICK Reviewed; 557 AA.
AC Q5ZHN9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial;
DE EC=2.7.8.5;
DE AltName: Full=Phosphatidylglycerophosphate synthase 1;
DE Short=PGP synthase 1;
DE Flags: Precursor;
GN Name=PGS1; ORFNames=RCJMB04_35a14;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC phosphatidylglycerol and cardiolipin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC -!- ACTIVITY REGULATION: Activated by calcium and magnesium and inhibited
CC by other bivalent cations. {ECO:0000250}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000305}.
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DR EMBL; AJ721095; CAG32754.1; -; mRNA.
DR RefSeq; NP_001008463.1; NM_001008463.1.
DR AlphaFoldDB; Q5ZHN9; -.
DR SMR; Q5ZHN9; -.
DR STRING; 9031.ENSGALP00000011616; -.
DR PaxDb; Q5ZHN9; -.
DR GeneID; 422087; -.
DR KEGG; gga:422087; -.
DR CTD; 9489; -.
DR VEuPathDB; HostDB:geneid_422087; -.
DR eggNOG; KOG3964; Eukaryota.
DR HOGENOM; CLU_030471_1_2_1; -.
DR InParanoid; Q5ZHN9; -.
DR OrthoDB; 1358866at2759; -.
DR PhylomeDB; Q5ZHN9; -.
DR TreeFam; TF314768; -.
DR UniPathway; UPA00084; UER00503.
DR PRO; PR:Q5ZHN9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586; PTHR12586; 1.
DR PROSITE; PS50035; PLD; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Repeat; Transferase; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..557
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase, mitochondrial"
FT /id="PRO_0000337109"
FT DOMAIN 212..238
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 461..494
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 557 AA; 63067 MW; 40296640BBAB1B7F CRC64;
MAAAGGAALW RRLAAWLPRG PPGLAALLGR LSDRLSRGRD RRSRRSSWLL LAPLLTPPVP
VITAMPCSLC PEGAHRFQWI RNLVPEFGIS SSHVKVLSSP AEFYELLKVQ IKTAKQRVVM
ASLYLGTGLL EQELVNCLEE TLEKSLQANE SPNLRVSILL DYTRGSRGRK NSRTMLIPLL
QRFPEQVRVS LFHTPNLRGL LKLLIPERFN ETIGLQHIKV YLFDDNVILS GANLSDLYFT
NRQDRYVLLQ DSPEIADFFT ELVDAIGDVS LQLQQDDTVQ MMEGMVHPYQ GDKVRYCEIA
NQRVMEVIDS ARTRQELLHA KTFHSSQQGS SMLPQHDSEA SEGLKPEPDT WIYPLIQMKP
FGIQIDEMVT ETLLTEAERD AKIYLTTGYF NLTQAYMDLI LGTRAEYRIL LASPEVNGFF
GAKGVAGAIP SAYVYIEHQF YNEVCCLHQQ ERVQLQEYSR AGWTFHAKGL WLYLAGSSLP
CLTLIGSPNF GYRSVHRDLE AQVAIVTENK ALQQQLHQEQ EQLYLCSGVV SSSTFEQPSR
HVKLWVKLVT PLIKNFF
