ID   BCHH_CERS4              Reviewed;        1193 AA.
AC   Q9RFD5; Q3J174;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Magnesium-chelatase subunit H;
DE            EC=6.6.1.1;
DE   AltName: Full=Mg-protoporphyrin IX chelatase subunit H;
GN   Name=bchH; OrderedLocusNames=RHOS4_18920; ORFNames=RSP_0287;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA   Choudhary M., Kaplan S.;
RT   "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT   sphaeroides 2.4.1.";
RL   Nucleic Acids Res. 28:862-867(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in bacteriochlorophyll pigment biosynthesis;
CC       introduces a magnesium ion into protoporphyrin IX to yield Mg-
CC       protoroporphyrin IX.
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; bacteriochlorophyll
CC       biosynthesis (light-independent).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC       {ECO:0000305}.
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DR   EMBL; AF195122; AAF24273.1; -; Genomic_DNA.
DR   EMBL; CP000143; ABA79460.1; -; Genomic_DNA.
DR   PIR; T50729; T50729.
DR   RefSeq; WP_011338125.1; NZ_CP030271.1.
DR   RefSeq; YP_353361.1; NC_007493.2.
DR   AlphaFoldDB; Q9RFD5; -.
DR   SMR; Q9RFD5; -.
DR   STRING; 272943.RSP_0287; -.
DR   EnsemblBacteria; ABA79460; ABA79460; RSP_0287.
DR   KEGG; rsp:RSP_0287; -.
DR   PATRIC; fig|272943.9.peg.2231; -.
DR   eggNOG; COG1429; Bacteria.
DR   OMA; WPETIAC; -.
DR   PhylomeDB; Q9RFD5; -.
DR   BioCyc; MetaCyc:MON-13264; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000002703; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd10150; CobN_like; 1.
DR   InterPro; IPR003672; CobN/Mg_chltase.
DR   InterPro; IPR022571; Mg_chelatase_H_N.
DR   PANTHER; PTHR44119; PTHR44119; 2.
DR   Pfam; PF02514; CobN-Mg_chel; 2.
DR   Pfam; PF11965; DUF3479; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW   Ligase; Nucleotide-binding; Photosynthesis; Reference proteome.
FT   CHAIN           1..1193
FT                   /note="Magnesium-chelatase subunit H"
FT                   /id="PRO_0000219886"
SQ   SEQUENCE   1193 AA;  129206 MW;  13DDEBD375223151 CRC64;
     MHGEVSGPAG TPGYSIAIVT LDAHAAGPAA RIAPRLQQDF PGLTLSIHAA AEWAEKPEAL
     AAAREAIGRA DIVIANLLFI EEHINAVLPE LQAARERVDA FVGMIADPSI VKLTKMGDLD
     MQKPASGPMA LLKKLRGASK EQGNSGESQM RMLRTIPKML KFVPGKAQDL RAWFLSMQYW
     LGGSDDNLEQ MVRYLVSRYS ANRAWHRIHA KAPIEYPEVG LYHPSLPDRI TTDPNDLPRP
     AGAKVTVGLL MLRSYILASD TAHYDAVIEA FERKGIAVLP AFAGGLDGRP AIDAYFHDKL
     GTTIDAMVSL TGFSLVGGPA YNDSHAAIEA LKGLDVPYIA AHPLEFQTLG QWAQAGGGLG
     PVETTMLVAL PEIDGATNPT VFAGRHDLSG CTGCPGGCKA TAQAAECRAM SPCHERIQTL
     AEKTLRLALL RRSKIAERRV GVVLYGFPPN AGAVGTAAYL AVFESLFNVL NAMKREGYQL
     EVPESVQALR DAVLGGTASQ YGQPANIAAH VSAEKIVSGT PWLADIEKAW GAAPGRIQSD
     GRGVYILGQQ FGNVFVGVQP VFGYEGDPMR LLFEKGFAPT HAFSVFYRWL REDFGADVLL
     HFGMHGALEF MPGKQAGMSG ACWPDRLIGA LPNVYLYAAN NPSEASLAKR RSNAITVTHL
     TPPLAKAGLY RGLQDLKDSL TRYRQLAPDA PEREELSLLI GEQARAVNLD MVDVDTMWLK
     LLETEGSLIT DGLHVVGRPM TEEQIADNIA LMPEMSSERR AEVEGMLRQE TEIAGLLRAL
     GGHYMEPVPG GDLIRAPEIL PTGRNIHAFD PFRMPTAYAI QDGAAQAQRL LDAHPKLPET
     VALVLWGSDN IKSDGGPIAQ ALALMGARPR FDHYGRLAGA DLIPLSELGR PRIDVIMTLS
     GIFRDLLPLQ TRMLAEAAWK AANAEGEPLA QNFIRAHALS YAQEMGVDME TASLRVFSNA
     EGAYGSNVNV LVGSSAFGEE DELADAYEAR KSFAYGRSGK PVQNAALLQK SLKTVDVAYQ
     NLESVELGVT TVDHYFDTLG GIARAVKRAR GEEASVYIGD QTRGGGTVRT LKDQIALETR
     ARSLNPKYYE GLLKHGAEGV RQIEAQVTNT LGWSATTQQV EPWVYQRLSE TFVLDEAMRR
     RLAELNPEAS VRMAERLLEA SARNYWQPDA ETLAALQGAA DELEDRLEGI AAE