ID A0A0N9N649_9ACTN Unreviewed; 673 AA.
AC A0A0N9N649;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:ALG86028.1};
GN ORFNames=ACH46_17910 {ECO:0000313|EMBL:ALG86028.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG86028.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG86028.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG86028.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
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DR EMBL; CP011853; ALG86028.1; -; Genomic_DNA.
DR RefSeq; WP_062394129.1; NZ_CP011853.1.
DR AlphaFoldDB; A0A0N9N649; -.
DR STRING; 1136941.ACH46_17910; -.
DR KEGG; goq:ACH46_17910; -.
DR PATRIC; fig|1136941.3.peg.3662; -.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000063789; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd01451; vWA_Magnesium_chelatase; 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; IPR041702; BchD/ChlD_VWA.
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; PTHR35023; CHELATASE-RELATED; 1.
DR PANTHER; PTHR35023:SF1; MG-PROTOPORPHYRIN IX CHELATASE; 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 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;
FT DOMAIN 491..627
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 292..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 70311 MW; E722CB443DBA3884 CRC64;
MSTPHYPFTA VVGADSLDEP QPMALALLLT AISPAVGGVL VRGEKGTAKS TIVRALAAVL
PPLDDAPVPL VELPVGATED RVIGSIDLET ALGEGKTRYQ PGLLAKAHRG LLYVDEVNLL
HDHLVDLLLD AAAMGRATVE RDGISMTHDA RFVLVGTMNP EEGELRPQLL DRFGLTVEVA
APREPAVRAE VVRRRMAYDA DPAGFAARYA DSEAALTTRI ATAQKLLPEV VLSSAALLKI
AEVGAAFDVD GLRADIVTAR TAVAHAAWCG RTAVTVDDIR VAARLALPHR RRRNPFDAPG
LDEDLLDQIL GDDDLPPDPP EGGGPGDDPA GDGGEADAGP STDAADGPAH STDDPADTAD
APPRSTADFA DTADAPPRWL SRSEAPAEDR VETAAGTQTT TTIPAGTPYR TRLLTVAGTG
AGTTGRRSRA KTSSGRRVGV DPAATAGAPH LVETIRAAIP HQHARGRTDG RLLIETSDLR
RAEYEGRESN LVLFCVDASG SMAARKRMAQ VKTAVLSLLL DAYQRRDKVG LVTFRGHDAE
VVLPPTGSVD VAAARLQDLP AGGRTPLAEG LTKVAELLAV ERIRDARRRP LLVVVTDGRA
TSGADAVARS HLAADRLAQQ GVASVVIDCE SGPLRLGLAA DLARHLGADY LEVGDVSAGD
LIAAARIATE GAA
//