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Database: UniProt
Entry: K9V7S7_9CYAN
LinkDB: K9V7S7_9CYAN
Original site: K9V7S7_9CYAN 
ID   K9V7S7_9CYAN            Unreviewed;       370 AA.
AC   K9V7S7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Cobalamin synthesis protein P47K {ECO:0000313|EMBL:AFZ03492.1};
GN   ORFNames=Cal6303_4592 {ECO:0000313|EMBL:AFZ03492.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ03492.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFZ03492.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ03492.1,
RC   ECO:0000313|Proteomes:UP000010477};
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., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-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; CP003610; AFZ03492.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9V7S7; -.
DR   STRING; 1170562.Cal6303_4592; -.
DR   KEGG; calt:Cal6303_4592; -.
DR   PATRIC; fig|1170562.3.peg.5019; -.
DR   eggNOG; COG0523; Bacteria.
DR   HOGENOM; CLU_017452_0_1_3; -.
DR   Proteomes; UP000010477; 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:UP000010477}.
FT   DOMAIN          280..368
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
FT   REGION          245..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  41915 MW;  AA48299DCF981B08 CRC64;
     MVYAKLSERL FIQLGDRMMQ SAVSPNQSPV MNSTKQGIPV TIITGFLGSG KTTLLNHILS
     NQQGLKTAVL VNEFGEIGID NELIVSTDEN MVELSNGCIC CTINTDLVDA VYKILERRDN
     IDYLVVETTG LADPLPVALT FLGTELRDLT RLDSIVTVVD AANYSLDLFN SEAAHSQIAY
     GDVILLNKTD LVTESELNNL ETKINQVKEG ARIIRTKNSQ VPLALILSVG LFASEKYFDL
     DEHHEHDHHH EHDHHEHDHE NCEHDHEHHH HSAHLENDGF TSISFQSDKP FGIRQFQYFL
     DNQLPTNIFR AKGIMWFEES PKRHIFHLCG KRFTMDDDEW KGEKKNQLVL IGQNLDQEAL
     LEQIKACVVE
//
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