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Database: UniProt
Entry: G0HRR6_HALHT
LinkDB: G0HRR6_HALHT
Original site: G0HRR6_HALHT 
ID   G0HRR6_HALHT            Unreviewed;       720 AA.
AC   G0HRR6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Protporphyrin IX magnesium chelatase {ECO:0000313|EMBL:AEM55899.1};
DE            EC=6.6.1.1 {ECO:0000313|EMBL:AEM55899.1};
GN   Name=hmcA {ECO:0000313|EMBL:AEM55899.1};
GN   OrderedLocusNames=HAH_0273 {ECO:0000313|EMBL:AEM55899.1};
OS   Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182
OS   / NCIMB 2187 / VKM B-1755).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=634497 {ECO:0000313|EMBL:AEM55899.1, ECO:0000313|Proteomes:UP000005629};
RN   [1] {ECO:0000313|EMBL:AEM55899.1, ECO:0000313|Proteomes:UP000005629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 /
RC   VKM B-1755 {ECO:0000313|Proteomes:UP000005629};
RX   PubMed=21994921; DOI=10.1128/JB.05953-11;
RA   Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., Wang S.,
RA   Xiang H.;
RT   "Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for
RT   studying genetics, metabolism, and virus-host interaction.";
RL   J. Bacteriol. 193:6086-6087(2011).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000256|ARBA:ARBA00005799}.
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DR   EMBL; CP002921; AEM55899.1; -; Genomic_DNA.
DR   RefSeq; WP_014039274.1; NC_015948.1.
DR   AlphaFoldDB; G0HRR6; -.
DR   STRING; 634497.HAH_0273; -.
DR   GeneID; 25155951; -.
DR   KEGG; hhi:HAH_0273; -.
DR   eggNOG; arCOG00438; Archaea.
DR   HOGENOM; CLU_016684_4_0_2; -.
DR   OrthoDB; 25914at2157; -.
DR   Proteomes; UP000005629; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045006; CHLI-like.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR   PANTHER; PTHR32039:SF9; MAGNESIUM-CHELATASE SUBUNIT CHLI-1, CHLOROPLASTIC; 1.
DR   Pfam; PF17863; AAA_lid_2; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13519; VWA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:AEM55899.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          549..720
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          321..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..386
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..449
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  75129 MW;  CB7CCBF5A800D777 CRC64;
     MVVLGDGKKA SQEASFAAVV GQRDLKDGLL AVATDDDLDG LLVRGEKGTA KSTAVRALAD
     LLPEQRAVAD CPYGCPPDRP EAQCDDCRTR ADPPVETRSV PLVTLPLGAT RDRVVGTLSV
     ADALDGDHEF DPGLLARANR GILYVDEVNL LDDHLVDVLL DAAASGQNRV ERDGVTVSHP
     AEFTLVGTMN PEEGDLRPQL RDRFALQTEV SACENLDDRV AIIDQALGED GDEEMQSEPD
     RDPGERLRTA RELLPEVALA REFREQIAEL CRDAGLDGHR GDIATARAAR TFAALDGRTT
     VLESDIERAA EFALPHRLTS RPFEDAPDVD DVLDDHFEDG EDESEEQSDD DGENGDEEGD
     AEDDGEEAGA GDESVNDGAD SEGGEDGSEQ QEQRPDDSGD AGEGGDDESG ERGEQPTPTS
     ADSDGERQEA EAGDGEGAAG DDGGEGESNQ SDDPENATPL LPGQSRATVG DSGAPDVDAP
     SVDTDGGSAS GRASATGTKR GATVRTERAG RDDEVDAAAS VRAAASRGSG HVESRDLRKS
     VRAGDAETLV VFAVDASASM RPAMKAAKGT VLELLKDAYQ ARDQVAFVTF AGEGADVVLP
     PTESVSLAAR HLKDLPTGDR TPLPDGLAAA REVLDRADPD AGVVVVVTDG RANTADGSPV
     AATRNAARTL GEAADRTVVV DAGEGSRAGL LDLVADETDA SVVPLDALTA ERVDAVASKR
//
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