ID A0A0F4R1T1_9GAMM Unreviewed; 598 AA.
AC A0A0F4R1T1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:KJZ13534.1};
GN ORFNames=TW85_12540 {ECO:0000313|EMBL:KJZ13534.1};
OS Marinomonas sp. S3726.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ13534.1, ECO:0000313|Proteomes:UP000033747};
RN [1] {ECO:0000313|EMBL:KJZ13534.1, ECO:0000313|Proteomes:UP000033747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3726 {ECO:0000313|EMBL:KJZ13534.1,
RC ECO:0000313|Proteomes:UP000033747};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ13534.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXYC01000013; KJZ13534.1; -; Genomic_DNA.
DR RefSeq; WP_046017478.1; NZ_JXYC01000013.1.
DR AlphaFoldDB; A0A0F4R1T1; -.
DR PATRIC; fig|579484.3.peg.2572; -.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000033747; Unassembled WGS sequence.
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 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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000033747}.
FT DOMAIN 32..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 284..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 66136 MW; 1D4121B44EAA649F CRC64;
MTSLPHFEFP FTAVAGQENF KLALTLAAIN PLLGGVLVSG PRGSAKSTLA RGLAHVLPDL
EAPFATLPLG ASEERLLGTL DLDKVLKNKE VAFHPGLLSK AHGGVLYVDE VNLLADNLVD
QLLDVAASGV NRVERDGISH EHAAKFILVG TMNPDEGELR PQLQDRFGLM VELANNYTLE
ERVQIVKLRD EFDQNPQAFC EKYRVKQKNL RQSIEIAQQK LPHIECSDEM RLLIAKACFQ
ANVDGVRADI VWLRAATAYT AWRGGKSVTR ADLDMVAELV LAHRRQVGSS SPPSAGSSTH
QDMIQKPNSS QNKTRRPDTS RLKDSHNPVE QNQQGQVDKQ DEDESQPNQT EDDWGSMPAQ
SQALDNNIRF DTKLESKRNN EFKTSIEEQS FFLSKGESAQ GKGLNNNLPG KAVNWHQTIS
QSADSEGFQW PPTKLHRQKA RTSQGMLHLI LLDCSASMLG QAVFGKAKGA ILDIAQQAYI
KREQIAMFIF GNNEVKQVQA KVRAPKDMSE FLNKIEAGGG TPFRDGLLEV ASWLTRYYKQ
SPMSVSHTYI FTDGRTQADV ADIELKGSCS LIDIEASAIK RGRAQQLAHA IKAEYFTI
//
