ID A0A372G7H3_9ACTN Unreviewed; 647 AA.
AC A0A372G7H3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN ORFNames=D0T12_32400 {ECO:0000313|EMBL:RFS81340.1};
OS Actinomadura spongiicola.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS81340.1, ECO:0000313|Proteomes:UP000262882};
RN [1] {ECO:0000313|EMBL:RFS81340.1, ECO:0000313|Proteomes:UP000262882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52907 {ECO:0000313|EMBL:RFS81340.1,
RC ECO:0000313|Proteomes:UP000262882};
RA Li L., Lin H.W.;
RT "Actinomadura spongicola sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-2018) 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:RFS81340.1}.
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DR EMBL; QVNQ01000014; RFS81340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372G7H3; -.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000262882; 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; IPR012804; Cob_chelat_sub_put.
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 NCBIfam; TIGR02442; Cob-chelat-sub; 1.
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:UP000262882}.
FT DOMAIN 475..605
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 315..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 68252 MW; B1DA71D38D612CE7 CRC64;
MNVTYPFTAV VGLDDLKLAL LLNAVSPRVG GVLVRGEKGT AKSTIVRALA AQLPAVDTVA
GCRFACDPAA PDPSCPDGPH APDGTSVRRP SALVELPVGA SEDRVAGSLD VERALTEGVK
AFEPGLLAAA HRGVLYVDEV NLLHDHLVDL LLDAAALGTC YVERESVSVR HAARFLLVGT
MNPEEGELRP QLLDRFGLTV EVRASREPKE RAEVVRRRLA FEADPAGFAE RWAAEEAALA
ERIAVARDRL ADVRLPDERL EQIATVCAGF EVDGMRADLV TANAALAHAA WHGRDTVTAD
DVRAAARLAL PHRRRRDPFD APGLDESLLD DLLNDSSPDD DPPPGGDDGG RDNNEQPPPS
NGAEGSAEPP APESEESGGG GGERVASAAA PHAVPLLEVP GVGDGVAGRR SRSRTVRGRV
TGARRPSGKV RDPHVVATLL AAAPHQRTRG RDGAGLVLRA DDLREADREG REGNLVLFVV
DASGSMAARR RMTTVKTAVL SLLLDAYQRR DKIGLITFRG RTADLVLPPT SSVEAGAARL
RALPTGGRTP LAAGLVRAAE VLRAERLRDP ARRPLLVVVT DGRATAEGDV ARAAGLLTGT
AGIVVDCEDG PVRLGLAGRL ATRLGARLVP LGDLDGIVRD QRRRKAA
//
