ID   A1BIS7_CHLPD            Unreviewed;      1280 AA.
AC   A1BIS7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   02-SEP-2026, entry version 77.
DE   RecName: Full=magnesium chelatase {ECO:0000256|ARBA:ARBA00012825};
DE            EC=6.6.1.1 {ECO:0000256|ARBA:ARBA00012825};
GN   OrderedLocusNames=Cpha266_2313 {ECO:0000313|EMBL:ABL66304.1};
OS   Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC   Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
OC   Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL66304.1, ECO:0000313|Proteomes:UP000008701};
RN   [1] {ECO:0000313|EMBL:ABL66304.1, ECO:0000313|Proteomes:UP000008701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 266 {ECO:0000313|EMBL:ABL66304.1,
RC   ECO:0000313|Proteomes:UP000008701};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=protoporphyrin IX + Mg(2+) + ATP + H2O = Mg-protoporphyrin IX
CC         + ADP + phosphate + 3 H(+); Xref=Rhea:RHEA:13961, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57306, ChEBI:CHEBI:60492,
CC         ChEBI:CHEBI:456216; EC=6.6.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00048693};
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}.
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DR   EMBL; CP000492; ABL66304.1; -; Genomic_DNA.
DR   RefSeq; WP_011746093.1; NC_008639.1.
DR   AlphaFoldDB; A1BIS7; -.
DR   STRING; 290317.Cpha266_2313; -.
DR   KEGG; cph:Cpha266_2313; -.
DR   eggNOG; COG1429; Bacteria.
DR   HOGENOM; CLU_002017_1_2_10; -.
DR   OrthoDB; 9757976at2; -.
DR   Proteomes; UP000008701; Chromosome.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:InterPro.
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   NCBIfam; NF009140; PRK12493.1; 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, ECO:0000313|EMBL:ABL66304.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008701}.
FT   DOMAIN          2..163
FT                   /note="Magnesium chelatase subunit H N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11965"
FT   DOMAIN          166..1258
FT                   /note="CobN/magnesium chelatase"
FT                   /evidence="ECO:0000259|Pfam:PF02514"
SQ   SEQUENCE   1280 AA;  144141 MW;  BCBBC5673B98AE8E CRC64;
     MRFVFLTMES TNNGTLRSAA ETLNQRFGLN LDVAIFNLGL HHAAPNLWEQ LEERFRTADF
     IFGSMLFSEE IVRPLEKLLE QALCPVCIIT SNPALITQTR VGKFSLRKSK EETKEPGLFK
     QWASKLKPKH SHGESQRQLA LARNVSRMMK HLPGKARDIH TFIAAHQFWL NGSEENMERF
     LSLLIDRYVP GWKGKLPQSD PVFYPEAGLC HPDAPEQFFS AGEYLQWQKK NHPSGGKGPV
     AILAMRSTML SKNMQHIDSL QKALESKGID TCIAYSGGLD FRPALDRFFD PQKPGTLRPR
     LLINATGFSL VGGPAETRAA EAVVAMNKLD VPCYNLIPLS FQHVEQWRES NLGLTPLQTA
     LSVAVPELDG TIEPHVYAGT EAGTDRTVPL KEEIAAVANR AHRFLRLQEK PVSEKKIAIV
     LFNFPPNLGN AGTAAYLNVF ESLIRLLKEM KTAGYHVDLP ASVEELKNKL LEGNRLIYGT
     DGNVADHLPV DEYRKRFPAY TEIEPFWGDA PGEILNDRQK FHILGCSFGN IFLGQQPGFG
     YERDPMRLLM AKDAAPNHAF AAFYTWIEQC FNADAVLHFG THGALEFMPG KQTGLSSSCW
     PKKLIGSLPN FYVYCVNNPS EGAIAKRRGY ATIISYLTPP LEHAGLYKEL ARLRALIAGT
     RQTTTHETMA EIRELASSLE LDTGLQELPD ETWLARLNSE LYLVEERMIP LGLHIMGEAP
     TPESLVDHLA LLTSHSRPEL DNRTLPELIC KHRHLDYHLL IERIKDDRDA QREWQELLAI
     TREAIKLFTR HLPDGQTTDH LPVRAMLEGT FTVRMAEADS YLHRQAGIKI GELQKLWHFL
     QRILVNLAEN REIHAVLHAL EGKYTPPSPG NDLVRNPDTV PTGRNIHSLD PYSIPTHFAQ
     QTGERSAEEL LQVYRDENGS LPESIAIVLW GTDNLKSDGE GVAQALALLG ARAKTDELGK
     IGDVELIPLE QLGRPRIDVV MTISGIFRDL LSHQVKLLDK AVRMAAAADE PESMNFLRKH
     VLQEMLEKNI PFSDASNRVF SNAPGSYGAN VNHLVESSTW EEEEQLVDAF VSRKSFAVTE
     TGQWKECPDA LRSALQHVTL TFQNIDSYEI GISDIDHYYE YLGGISKTVE QISKTMPKVM
     IGDINGFGKK QRICSLEKMV SLEARTKLLN PKWYEAMLEH GYEGVREIES HLTNTYGWSA
     TASAVKEWTY RQFSETFLQD KAMLERLASM NVHATRAMTS RLLEAHSRGF WDADAETIEE
     LREIYLDLET KIEGVHHETH
//