ID W7IT98_9PSEU Unreviewed; 677 AA.
AC W7IT98;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN ORFNames=UO65_0547 {ECO:0000313|EMBL:EWC64115.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC64115.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC64115.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC64115.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
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:EWC64115.1}.
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DR EMBL; AYXG01000021; EWC64115.1; -; Genomic_DNA.
DR RefSeq; WP_035278390.1; NZ_AYXG01000021.1.
DR AlphaFoldDB; W7IT98; -.
DR STRING; 909613.UO65_0547; -.
DR PATRIC; fig|909613.9.peg.562; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR041702; BchD/ChlD_VWA.
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; PTHR35023; CHELATASE-RELATED; 1.
DR PANTHER; PTHR35023:SF1; MG-PROTOPORPHYRIN IX CHELATASE; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277}.
FT DOMAIN 493..633
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 334..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 69794 MW; 7C90FE32C81B986C CRC64;
MPSPAGFPFS AVVGHADLRL SLLLNAVHPA IGGVLVRGEK GTAKSTVVRA LAALLPALAV
VEGCRFGCDP AAPDPGCPDG PHLEPDAASR PARLVELPVG ATEDRLIGSL DLERALTEGV
RAYQPGLLAA AHRGVLYVDE VNLLHDHLVD LLLDAAAMGR AHVEREGVSV AHAASFLLVG
TMNPEEGELR PQLLDRFGLT VEVRAARDVD TRTEVIRRRL AFEADPAGFA AGWAAADADL
AARIAAARAA LPGVALPDAE LRRIAAVCAA FDVDGMRADL VLARAAIAHA AWRGADAVTE
EDVAVAARLA LPHRRRRDPF DEPGIEQDQL DQALRDAAEQ TGEPERTDPD PDPDPGPDGP
GGGAPDPGDG PADDSGQSDS PPPDGPAPEG QDTQPKGKGG GTQAPATPDP AFTARLLQVD
GVGEGAPGRR SRSRAGSGRA LRAATSQGSG IHLVGTMTAA APMQLVRGRS GPGLVVRPDD
VRRAVREGRE SNLVLFVVDA SGSMAARKRM SAVTGAVISL LRDAYQRRDK VGLVTFRGPG
AEVALPPTSS VEAAVARLRA LRTGGRTPLA DGLLRARELL RVERLRDPRR RALLVVVTDG
RATVAARPGG DAVADAVRAA GLVAADGVAS VVVDCESGPV RLGLAGRVSA ALGGTGLRLE
ELSADAVAGV VRAARAA
//