ID   A4CVA1_SYNPV            Unreviewed;      1335 AA.
AC   A4CVA1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=magnesium chelatase {ECO:0000256|ARBA:ARBA00012825};
DE            EC=6.6.1.1 {ECO:0000256|ARBA:ARBA00012825};
GN   ORFNames=WH7805_04001 {ECO:0000313|EMBL:EAR17922.1};
OS   Synechococcus sp. (strain WH7805).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR17922.1, ECO:0000313|Proteomes:UP000001224};
RN   [1] {ECO:0000313|EMBL:EAR17922.1, ECO:0000313|Proteomes:UP000001224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224};
RA   Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F.,
RA   Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., Post A.,
RA   Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K.,
RA   Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001499};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism.
CC       {ECO:0000256|ARBA:ARBA00023444}.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC       {ECO:0000256|ARBA:ARBA00010851}.
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:EAR17922.1}.
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DR   EMBL; AAOK01000004; EAR17922.1; -; Genomic_DNA.
DR   RefSeq; WP_006041613.1; NZ_CH724168.1.
DR   STRING; 59931.WH7805_04001; -.
DR   eggNOG; COG1429; Bacteria.
DR   HOGENOM; CLU_002017_1_2_3; -.
DR   OrthoDB; 9757976at2; -.
DR   PhylomeDB; A4CVA1; -.
DR   Proteomes; UP000001224; Unassembled WGS sequence.
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-KW.
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   NCBIfam; TIGR02025; BchH; 1.
DR   PANTHER; PTHR44119; MAGNESIUM-CHELATASE SUBUNIT CHLH, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR44119:SF1; MAGNESIUM-CHELATASE SUBUNIT CHLH, CHLOROPLASTIC; 1.
DR   Pfam; PF02514; CobN-Mg_chel; 1.
DR   Pfam; PF11965; DUF3479; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531}.
FT   DOMAIN          25..187
FT                   /note="Magnesium chelatase subunit H N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11965"
SQ   SEQUENCE   1335 AA;  148145 MW;  CB8252B9BE17B28D CRC64;
     MFTQVRSADR RVAPVEGQNH KSVMKAVYVV LEPQYQNSLT QAATALNAAE GDLGIDLCGY
     LIEELRDPDN YENFKQDVSE ADVFIASLIF IEDLAQKVVE AVAPHRDRLK AAVVFPSMPE
     VMRLNKLGSF SMAQLGQSKS AIAGFMKKRK EAGGAGFQDA MLKLLNTLPT VLKYLPVEKA
     QDARSFMLSF QYWLGGTPDN LRNFLLMLAD KYVFPAVEGE ERPAMEVAEP EVFPDLGIWH
     PLAPTMFEDL KEYLNWTSSR TDLSDEAWQG PVIGLVLQRS HIVTGDDAHY VAVVQELEFR
     GARVIPIFCG GLDFSKPVNA FFYDPLNPEQ PLVDGIVSLT GFALVGGPAR QDHPKAIESL
     KKLNRPYMVA LPLVFQTTQE WEDSDLGLHP VQVALQIAIP ELDGAIEPIV LSGRDDATGK
     AHTLQDRVDA IAERAIRWSS LRIKPRNQKK LAITVFSFPP DKGNVGTAAY LDVFGSIHRV
     LEEMKAKGYD IQDLPRDSKT LMEAVINDPE AMQGAPELSI AHRMSVEEYE RLTPYSERLE
     ENWGKPPGNL NSDGQNLLIY GRHFGNVFVG VQPTFGYEGD PMRLLYSRSA SPHHGFAAYY
     TYLEKVWRAD AVLHFGTHGS LEFMPGKQMG MSETCYPDSL IGSLPNLYYY AANNPSEATI
     AKRRGYASTI SYLTPPAENA GLYKGLKELG ELVGSYQQLR EGGRGVQIVN TIVETARQCN
     LDKDVDLPED DAASLDLDGR DALVGAVYRQ LMEIESRLLP CGLHTIGKPP TAEEAVATLV
     NIAALEREED GLRSLPGLLA EAMGRTIEDI YRGNDEGVLA DVELNRTITE TSRAAIGSMV
     RSLTGLDGRV NMRGNFGWLL DLLTKFGLKL PTPWLRACCG AGFTSIDSTE LDKLFAYLRF
     CLEQICADME MESLLRALDG EYVLPGPGGD PIRNPGVLPS GKNIHALDPQ AIPTRAAVAA
     AKGVVDKLIE RQREEQGTWP ETIACVLWGT DNIKTYGESL AQILWFVGVK PMADSVGRVN
     KLELIPLEEL GRPRIDVVVN CSGVFRDLFI NQMALIDQAV KMAAEADEPL EQNFVRRHAL
     EQAEKEGTSL RDAACRVFSN ASGSYSSNVN LAVENSTWEE EGELQEMYLS RKTFAFNADN
     PGEMNQKRDV FENVMKTADV TFQNLDSAEI SLTDVSHYFD SDPTKLIKGL RDDGKAPTSY
     IADTTTANAQ VRSLSETIRL DSRTKLLNPK WYEGMLDSGY EGVREVAKRL NFTLGWSATS
     GAVDNFVYEE ANDTFINDPE MRKRLLELNP HSFRRIVGTL LEVNGRGYWE TSDENIQQLQ
     ELYQEVEDRI EGVTS
//