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Database: UniProt
Entry: K9PHC9_9CYAN
LinkDB: K9PHC9_9CYAN
Original site: K9PHC9_9CYAN 
ID   K9PHC9_9CYAN            Unreviewed;       370 AA.
AC   K9PHC9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Cobalamin synthesis protein P47K {ECO:0000313|EMBL:AFY32204.1};
GN   ORFNames=Cal7507_1747 {ECO:0000313|EMBL:AFY32204.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY32204.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY32204.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY32204.1,
RC   ECO:0000313|Proteomes:UP000010390};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003943; AFY32204.1; -; Genomic_DNA.
DR   RefSeq; WP_015128021.1; NC_019682.1.
DR   AlphaFoldDB; K9PHC9; -.
DR   STRING; 99598.Cal7507_1747; -.
DR   KEGG; calo:Cal7507_1747; -.
DR   PATRIC; fig|99598.3.peg.1957; -.
DR   eggNOG; COG0523; Bacteria.
DR   HOGENOM; CLU_017452_0_1_3; -.
DR   OrthoDB; 504781at2; -.
DR   Proteomes; UP000010390; 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:UP000010390}.
FT   DOMAIN          269..357
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
FT   REGION          224..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  41522 MW;  9915DD4A3B29883C CRC64;
     MPSAVTSEFP ALDAPKQGLP VTIITGFLGS GKTTLLNHIL TNQQGLKTAV LVNEFGEIGI
     DNELIVSTGE NMVELNNGCI CCTINNDLVD AVYKVLEREE KLDYLVVETT GLADPLPVAL
     TFLGTELRDL TRLDSIITVV DAANYSLDLF NSQAAYSQIA YGDVIILNKA DLVDEAALND
     LEKKIGEVKE GARILRTTRS EVPLPLILSV GLFESDKYFD AADEHDHKHD HHDHDHHDHD
     HSACSHEHHD HEHDHDHHNH SDHLENDGFT SISFQSDKPF SIRKFQYFLD NQLSTNIFRA
     KGIMWFDESP KRHIFHLCGK RFTMDDDEWK GEPKNQLVLI GQNLDHETLL TQLENCICLP
     STSRGKGFGK
//
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