CHLG_AVESA
ID CHLG_AVESA Reviewed; 378 AA.
AC Q9M3W5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Chlorophyll synthase, chloroplastic;
DE EC=2.5.1.62;
DE AltName: Full=Polyprenyl transferase;
DE Flags: Precursor;
GN Name=CHLG;
OS Avena sativa (Oat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Aveninae; Avena.
OX NCBI_TaxID=4498;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INHIBITION BY N-PHENYLMALEIMIDE AND
RP DIACETYL, AND MUTAGENESIS OF ARG-91; CYS-109; CYS-130; CYS-137; ARG-151;
RP ARG-161; CYS-262; ARG-284 AND CYS-304.
RX PubMed=11501754; DOI=10.1515/bc.2001.112;
RA Schmid H.C., Oster U., Koegel J., Lenz S., Ruediger W.;
RT "Cloning and characterisation of chlorophyll synthase from Avena sativa.";
RL Biol. Chem. 382:903-911(2001).
RN [2]
RP CHARACTERIZATION, AND MUTAGENESIS OF ASN-146; ASP-147; ASP-150; ASP-154 AND
RP ARG-161.
RC STRAIN=cv. Pirol;
RX PubMed=12530542; DOI=10.1515/bc.2002.198;
RA Schmid H.C., Rassadina V., Oster U., Schoch S., Ruediger W.;
RT "Pre-loading of chlorophyll synthase with tetraprenyl diphosphate is an
RT obligatory step in chlorophyll biosynthesis.";
RL Biol. Chem. 383:1769-1778(2002).
CC -!- FUNCTION: Involved in one of the last steps of the biosynthesis of
CC chlorophyll a. Catalyzes the esterification of chlorophillide a with
CC either geranylgeranyldiphosphate (GGPP) or phytyldiphosphate (PhyPP).
CC May also use with a lower efficiency the monophosphates GGMP and PhyMP,
CC but not the non-phosphorylated alcohols geranylgeraniol and phytol. The
CC tetraprenyl diphosphate must bind to the enzyme as the first substrate
CC and esterification occurs when this pre-loaded enzyme meets the second
CC substrate, chlorophyllide. {ECO:0000269|PubMed:11501754}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyllide a + H(+) + phytyl diphosphate = chlorophyll a +
CC diphosphate; Xref=Rhea:RHEA:17317, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58416, ChEBI:CHEBI:75434,
CC ChEBI:CHEBI:83348; EC=2.5.1.62;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Magnesium or zinc; or manganese at a lesser extent, but not
CC calcium.;
CC -!- ACTIVITY REGULATION: Inhibited by N-phenylmaleimide (NPM) and diacetyl.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed in etiolated and green
CC seedlings.
CC -!- DOMAIN: The N-terminal part (1-87) is not required for enzymatic
CC activity.
CC -!- DOMAIN: Amino acid residues 138-160 are probably part of the polyprenyl
CC diphosphate-binding domain.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. Chlorophyll
CC synthase subfamily. {ECO:0000305}.
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DR EMBL; AJ277210; CAB85464.1; -; mRNA.
DR AlphaFoldDB; Q9M3W5; -.
DR SMR; Q9M3W5; -.
DR KEGG; ag:CAB85464; -.
DR BioCyc; MetaCyc:MON-11751; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046408; F:chlorophyll synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd13958; PT_UbiA_chlorophyll; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR006372; Chl_synth.
DR InterPro; IPR011799; ChlG.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR02056; ChlG; 1.
DR TIGRFAMs; TIGR01476; chlor_syn_BchG; 1.
PE 1: Evidence at protein level;
KW Chlorophyll biosynthesis; Chloroplast; Membrane; Plastid; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..378
FT /note="Chlorophyll synthase, chloroplastic"
FT /id="PRO_0000285116"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 91
FT /note="R->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:11501754"
FT MUTAGEN 109
FT /note="C->A: Reduces activity by 90%."
FT /evidence="ECO:0000269|PubMed:11501754"
FT MUTAGEN 130
FT /note="C->A: Reduces activity by 70%."
FT /evidence="ECO:0000269|PubMed:11501754"
FT MUTAGEN 137
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11501754"
FT MUTAGEN 146
FT /note="N->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12530542"
FT MUTAGEN 147
FT /note="D->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12530542"
FT MUTAGEN 150
FT /note="D->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12530542"
FT MUTAGEN 151
FT /note="R->A: Reduces activity by 75%."
FT /evidence="ECO:0000269|PubMed:11501754"
FT MUTAGEN 154
FT /note="D->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:12530542"
FT MUTAGEN 161
FT /note="R->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:11501754,
FT ECO:0000269|PubMed:12530542"
FT MUTAGEN 161
FT /note="R->H: Reduces activity by 99%."
FT /evidence="ECO:0000269|PubMed:11501754,
FT ECO:0000269|PubMed:12530542"
FT MUTAGEN 161
FT /note="R->K: Reduces activity by 66%."
FT /evidence="ECO:0000269|PubMed:11501754,
FT ECO:0000269|PubMed:12530542"
FT MUTAGEN 262
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11501754"
FT MUTAGEN 284
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11501754"
FT MUTAGEN 304
FT /note="C->A: Loss of inhibition by N-phenylmaleimide, but
FT no loss of activity."
FT /evidence="ECO:0000269|PubMed:11501754"
SQ SEQUENCE 378 AA; 40764 MW; B7FEABF82D061DE4 CRC64;
MATSHPLAAA AATSSSSATF RPPLRFLSSP PSSLTLNRRR SFPVVCAADA DAKETTKKPT
IPDKAPAAGS SFNQLLGIKG AKQETNIWKI RLQLTKPVTW PPLVWGVLCG AAASGNFHWT
VEDVTKSIVC MLMSGPCLTG YTQTINDWYD RDIDAINEPY RPIPSGAISE NEVITQIWVL
LLGGLGLGAL LDIWAGHDFP IIFYLALGGS LLSYIYSAPP LKLKQNGWIG NFALGASYIG
LPWWAGQALF GTLTPDIVVL TCLYSIAGLG IAIVNDFKSI EGDRTLGLQS LPVAFGMETA
KWICVGAIDI TQLSVAAYLL STGKLYYALA LLGLTIPQVI LQFQYFLKDP VKYDVKYQAS
AQPFFVFGLL VTALATSH
