CHLH_ORYSJ
ID CHLH_ORYSJ Reviewed; 1387 AA.
AC Q10M50; Q0DSA2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Magnesium-chelatase subunit ChlH, chloroplastic;
DE Short=Mg-chelatase subunit H;
DE EC=6.6.1.1;
DE AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlH;
DE Flags: Precursor;
GN Name=CHLH; OrderedLocusNames=Os03g0323200, LOC_Os03g20700;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22226678; DOI=10.1016/j.febslet.2011.12.026;
RA Zhou S., Sawicki A., Willows R.D., Luo M.;
RT "C-terminal residues of oryza sativa GUN4 are required for the activation
RT of the ChlH subunit of magnesium chelatase in chlorophyll synthesis.";
RL FEBS Lett. 586:205-210(2012).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC The reaction takes place in two steps, with an ATP-dependent activation
CC followed by an ATP-dependent chelation step. May be involved in the
CC plastid-to-nucleus retrograde signaling. {ECO:0000269|PubMed:22226678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-
CC protoporphyrin IX + phosphate; Xref=Rhea:RHEA:13961,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306,
CC ChEBI:CHEBI:60492, ChEBI:CHEBI:456216; EC=6.6.1.1;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC of subunits CHLI, CHLD, AND CHLH. {ECO:0000269|PubMed:22226678}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC Plastid, chloroplast membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Stromal side {ECO:0000250}. Plastid, chloroplast
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=Predominantly associated with the
CC chloroplast envelope. Spans the chloroplast envelope and its N- and C-
CC termini are exposed to the cytosol (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF11886.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000009; ABF95686.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF95687.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11886.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015631165.1; XM_015775679.1.
DR RefSeq; XP_015631166.1; XM_015775680.1.
DR AlphaFoldDB; Q10M50; -.
DR SMR; Q10M50; -.
DR STRING; 4530.OS03T0323200-02; -.
DR PaxDb; Q10M50; -.
DR PRIDE; Q10M50; -.
DR KEGG; osa:4332690; -.
DR eggNOG; ENOG502QT3B; Eukaryota.
DR HOGENOM; CLU_002017_1_1_1; -.
DR InParanoid; Q10M50; -.
DR OrthoDB; 64867at2759; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10M50; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd10150; CobN_like; 1.
DR InterPro; IPR011771; BchH.
DR InterPro; IPR003672; CobN/Mg_chltase.
DR InterPro; IPR022571; Mg_chelatase_H_N.
DR PANTHER; PTHR44119; PTHR44119; 1.
DR Pfam; PF02514; CobN-Mg_chel; 1.
DR Pfam; PF11965; DUF3479; 1.
DR TIGRFAMs; TIGR02025; BchH; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chlorophyll biosynthesis; Chloroplast; Ligase; Membrane;
KW Nucleotide-binding; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..1387
FT /note="Magnesium-chelatase subunit ChlH, chloroplastic"
FT /id="PRO_0000418766"
SQ SEQUENCE 1387 AA; 153470 MW; E453AE49A130FA5F CRC64;
MSSLVSTPFT TATGVQKKLG APVPLHSFLL SRRQPAAGAG RGRAAAAAIR CAVAGNGLFT
QTKPEVRRVV PPEGDASRRG VPRVKVVYVV LEAQYQSSVT AAVRELNADP RRAAGFEVVG
YLVEELRDEE TYKTFCADLA DANVFIGSLI FVEELALKVK DAVEKERDRM DAVLVFPSMP
EVMRLNKLGS FSMSQLGQSK SPFFQLFKRK KNSGGFADSM LKLVRTLPKV LKYLPSDKAQ
DARLYILSLQ FWLGGSPDNL QNFLKMIAVS YVPALKGADI KYDDPVLFLD AGIWHPLAPT
MYDDVKEYLN WYGTRRDTND KLKDPNAPVI GLVLQRSHIV TGDDGHYVAV IMELEAKGAK
VIPIFAGGLD FSGPTQRYLV DPITGKPFVN AVVSLTGFAL VGGPARQDHP KAIAALQKLD
VPYIVALPLV FQTTEEWLNS TLGLHPIQVA LQVALPELDG GMEPIVFAGR DPRTGKSHAL
HKRVEQLCTR AIRWAELKRK TKEEKKLAIT VFSFPPDKGN VGTAAYLNVF NSIYSVLQDL
KKDGYNVEGL PDTAEALIEE VIHDKEAQFN SPNLNVAYRM NVREYQSLTS YASLLEENWG
KPPGNLNSDG ENLLVYGKQY GNVFIGVQPT FGYEGDPMRL LFSKSASPHH GFAAYYTFVE
KIFQADAVLH FGTHGSLEFM PGKQVGMSDA CYPDSLIGNI PNIYYYAANN PSEATVAKRR
SYANTISYLT PPAENAGLYK GLKQLSELIS SYQSLKDTGR GPQIVSSIIS TAKQCNLDKD
VPLPEEGVEL PPNERDLIVG KVYAKIMEIE SRLLPCGLHV IGEPPSAIEA VATLVNIASL
DRPEDEIYSL PNILAQTVGR NIEDVYRGSD KGILADVELL RQITEASRGA ITTFVERTTN
NKGQVVDVTN KLSTMLGFGL SEPWVQHLSK TKFIRADREK LRTLFTFLGE CLKLIVADNE
LGSLKLALEG SYVEPGPGGD PIRNPKVLPT GKNIHALDPQ AIPTTAALKS AKIIVDRLLE
RQKVDNGGKY PETIALVLWG TDNIKTYGES LAQVLWMIGV RPVADTFGRV NRVEPVSLEE
LGRPRIDVVI NCSGVFRDLF INQMNLLDRA VKMVAELDEP EEMNYVRKHA QEQARELGVS
LREAATRVFS NASGSYSSNV NLAVENASWT DEKQLQDMYL SRKSFAFDCD APGAGMREQR
KTFELALATA DATFQNLDSS EISLTDVSHY FDSDPTKLVQ GLRKDGRAPS SYIADTTTAN
AQVRTLSETV RLDARTKLLN PKWYEGMMKS GYEGVREIEK RLTNTVGWSA TSGQVDNWVY
EEANATFIED EAMRKRLMDT NPNSFRKLVQ TFLEASGRGY WETSEENLEK LRELYSEVED
KIEGIDR