ID B0CDI4_ACAM1 Unreviewed; 324 AA.
AC B0CDI4;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Cobalamin synthesis protein/P47K {ECO:0000313|EMBL:ABW28053.1};
GN OrderedLocusNames=AM1_3057 {ECO:0000313|EMBL:ABW28053.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW28053.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW28053.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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DR EMBL; CP000828; ABW28053.1; -; Genomic_DNA.
DR RefSeq; WP_012163484.1; NC_009925.1.
DR AlphaFoldDB; B0CDI4; -.
DR STRING; 329726.AM1_3057; -.
DR KEGG; amr:AM1_3057; -.
DR eggNOG; COG0523; Bacteria.
DR HOGENOM; CLU_017452_1_1_3; -.
DR OrthoDB; 9808822at2; -.
DR Proteomes; UP000000268; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03112; CobW-like; 1.
DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR011629; CobW-like_C.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13748:SF65; 47 KD PROTEIN; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; CobW_C; 1.
DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000268}.
FT DOMAIN 234..322
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
SQ SEQUENCE 324 AA; 36820 MW; BD9F3843C9E846F3 CRC64;
MLPVPGLFEY RLPVTLITGF LGSGKTTLLN HLMRHLRDRR AAVFVNEFGA IDIDSQILVT
VDEDLVALSN GCICCQIRDD FLMAFRRVLA YNQMQTSAGK RGLDAIFLET SGVADPYPLM
LTFRATELWS LTRLDAILTV VDAETFTAEY FQSQAALAQI QHGDIILLNK TDLVDDEQLR
SVETEIQRFK PQARILPMTY GQVPLSSVLD VDLYSEDMST DSPSGVQHLQ NDGFVAVPFE
SDRPFSLRKF QKFLDYQLPS EVFRAKGVLW FDESPHRHLF QLSGKRSQLQ DEAWQDPPRN
QLVCIGRNLD EEELQHQLHQ CLAP
//