ID A0A0P4UV03_9CYAN Unreviewed; 508 AA.
AC A0A0P4UV03;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Mg(2+) chelatase family protein / ComM-related protein {ECO:0000313|EMBL:GAP96461.1};
GN ORFNames=NIES2104_29980 {ECO:0000313|EMBL:GAP96461.1};
OS Leptolyngbya sp. NIES-2104.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP96461.1, ECO:0000313|Proteomes:UP000052243};
RN [1] {ECO:0000313|EMBL:GAP96461.1, ECO:0000313|Proteomes:UP000052243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP96461.1,
RC ECO:0000313|Proteomes:UP000052243};
RX PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA Kawachi M.;
RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL DNA Res. 22:403-412(2015).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium
CC ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC {ECO:0000256|ARBA:ARBA00003398}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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:GAP96461.1}.
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DR EMBL; BBWW01000001; GAP96461.1; -; Genomic_DNA.
DR RefSeq; WP_058998712.1; NZ_BBWW01000001.1.
DR AlphaFoldDB; A0A0P4UV03; -.
DR STRING; 1552121.NIES2104_29980; -.
DR InParanoid; A0A0P4UV03; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000052243; 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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR004482; Mg_chelat-rel.
DR InterPro; IPR025158; Mg_chelat-rel_C.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
DR PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR Pfam; PF13541; ChlI; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF13335; Mg_chelatase_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
FT DOMAIN 213..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 508 AA; 55036 MW; B665548255E1F4B0 CRC64;
MLARVWSASL VGIDAVKVGV EVDVAGGLPG IVVVGLPGTE IQESKERVRT AIKNAGFAFP
MRRIVINLAP ADLRKEGPSF DLPISIGILA ASDQVAVESL ENYLFLGEVS LDGSLRPVAG
VLAIAAAAKS LGISNLVVPA DNVREAAVVK DLNVYGFKHL SEVGAFLNDS SGYIPARIDG
ELELAEMQFS APDLRDVKGQ AHARRALEIA AAGGHNLIFV GPPGSGKTML ARRLPGIMPP
LEFQEALEVT QIHSVAGLLK EKGSLIGVRP FRSPHHSASG AALVGGGTFP RPGEISLAHR
GILFLDELTE FRRDVLEFLR QPLEDGSVTI SRTRQSVSFP AQFTLVASTN PCPCGFYADT
VQACTCSPRA REQYWARLSG PLMDRIDLQV GVNRLKPEEI TQQPTGEDSE TVRERVQQAR
DRASQRFQNT PLRCNAEMQS AHLREWCKLD NGTRSLLENA IRRLGLSVRA SDRILKVART
IADLAGDNDL QTPHVAEAIQ YRTIDRMQ
//
