ID   A8G599_PROM2            Unreviewed;       449 AA.
AC   A8G599;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Cobalamin synthesis protein/P47K {ECO:0000313|EMBL:ABV50780.1};
GN   OrderedLocusNames=P9215_11651 {ECO:0000313|EMBL:ABV50780.1};
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV50780.1, ECO:0000313|Proteomes:UP000002014};
RN   [1] {ECO:0000313|EMBL:ABV50780.1, ECO:0000313|Proteomes:UP000002014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV50780.1,
RC   ECO:0000313|Proteomes:UP000002014};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000825; ABV50780.1; -; Genomic_DNA.
DR   RefSeq; WP_012007859.1; NC_009840.1.
DR   AlphaFoldDB; A8G599; -.
DR   STRING; 93060.P9215_11651; -.
DR   KEGG; pmh:P9215_11651; -.
DR   eggNOG; COG0523; Bacteria.
DR   HOGENOM; CLU_017452_0_0_3; -.
DR   OrthoDB; 517607at2; -.
DR   Proteomes; UP000002014; 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:SF62; COBW DOMAIN-CONTAINING 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}.
FT   DOMAIN          355..448
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   449 AA;  50864 MW;  87A74D927F76598C CRC64;
     MSIKDKVPVT ILTGFLGSGK TTLLNRILSE EHGKRIAVIE NEYGEVGIDQ GLVINADEEV
     FEMSNGCICC TVRGDLIRVL GNLMKRRDKF DYVLVETTGL ADPGPVAQTF FMDEEISSEF
     TLDGIVTLVD AAHIDQQLGR SDESSEQVAF ADVLVLNKTD LVSDDALNTL ESRLRDMNRM
     TRIIRAENAK VPIESVLNLS AFDLDQILKR RPTFLEPEYP FEWTGVYDLD AGKYELMLEE
     GPDPEMSLVA LVNQGESEEE LKDGAESSVR LYAEKANTLE PGNTIPYGEH INLKLDDKGN
     KSFILNIEKP TKIGLFTQHT AEEFNMKVIK REENKEIPFN TERFWQAEHE HDDEVGSIAI
     ERFGDVDPEK LNTWMGRLLS EKGVDIFRTK GFISYSGNPR RIVFQGVHML FTAQPDKEWG
     NEPRRNQLVF IGRNLNEKEM QEGFDKCLI
//