ID A0A0P7YPS8_9GAMM Unreviewed; 573 AA.
AC A0A0P7YPS8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Magnesium chelatase subunit D {ECO:0000313|EMBL:KPQ23767.1};
DE EC=6.6.1.1 {ECO:0000313|EMBL:KPQ23767.1};
GN Name=chlD {ECO:0000313|EMBL:KPQ23767.1};
GN ORFNames=HLUCCA13_12525 {ECO:0000313|EMBL:KPQ23767.1};
OS Halomonas sp. HL-48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1479235 {ECO:0000313|EMBL:KPQ23767.1, ECO:0000313|Proteomes:UP000050569};
RN [1] {ECO:0000313|EMBL:KPQ23767.1, ECO:0000313|Proteomes:UP000050569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-48 {ECO:0000313|EMBL:KPQ23767.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
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:KPQ23767.1}.
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DR EMBL; LJZS01000015; KPQ23767.1; -; Genomic_DNA.
DR RefSeq; WP_027336040.1; NZ_LJZS01000015.1.
DR AlphaFoldDB; A0A0P7YPS8; -.
DR STRING; 1479235.GCA_000686925_01037; -.
DR PATRIC; fig|1479235.4.peg.361; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000050569; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR CDD; cd00009; AAA; 1.
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; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
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; PF07728; AAA_5; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KPQ23767.1}.
FT DOMAIN 27..168
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 283..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 60902 MW; D67966D46412DE45 CRC64;
MSEFPFAAVV GQEALKTALI LNAINPRISG VLISGPRGSA KSTLARALAA ILPGDSDGQR
APFVTLPLGA SEDRLVGSLD LQKVLANGEA TFHAGLLAKA DGGVLYVDEV NLLPDTLVDL
LLDVAASGTN IVERDGISHS HPARFSLIGT MNPDEGELRP QLLDRFGLCI EQAASISVEE
RIAIVQQREA FDRDPAGAAR GFEEAQAALT ERIHQAQRQL AEVTTPSWVY QAIASRCEAA
GVEGLRADVT WHRAARAHAA WRGVGEVTQQ DIDTVEPWVL DHRRTQSPEP TPPSSPPPKE
PPSRGEGGSS STTNTSPGGS SNQCGEQGQW GAMPPQSQST IQQAAPELAN TPNGVGQAKT
AATPASGEKG QVSGKGRSRT ETSRLDGFAT LIANRGQWPW RKLKMRKTQA GQPRAHLVLL
DTSGSTLGQR LLGQAKGLVE ALVRQAYAAR EQVAVVGFGN GGVVPLLSRQ RAPKRVEAAL
EAATGGGGTP LREAVIEAKR LIHQWQRREP GLHIRTYLIT DGRTRESVAD LGPLDDCILL
DTESSKIKRG QGARIAQQLG ARYATPFSGQ ETP
//
