ID   COBW_SINSX              Reviewed;         354 AA.
AC   P29937;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein CobW;
GN   Name=cobW;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=1655697; DOI=10.1128/jb.173.19.6074-6087.1991;
RA   Crouzet J., Levy-Schil S., Cameron B., Cauchois L., Rigault S.,
RA   Rouyez M.-C., Blanche F., Debussche L., Thibaut D.;
RT   "Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair
RT   Pseudomonas denitrificans DNA fragment containing five cob genes and
RT   identification of structural genes encoding Cob(I)alamin
RT   adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide
RT   kinase-cobinamide phosphate guanylyltransferase.";
RL   J. Bacteriol. 173:6074-6087(1991).
CC   -!- FUNCTION: Might be involved in cobalt reduction leading to cobalt(I)
CC       corrinoids.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. CobW
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was orginally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M62866; AAA25779.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29937; -.
DR   SMR; P29937; -.
DR   KEGG; ag:AAA25779; -.
DR   UniPathway; UPA00148; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1220.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR012824; Cbl_biosynth_CobW.
DR   InterPro; IPR011629; Cbl_biosynth_CobW-like_C.
DR   InterPro; IPR036627; CobW-likC_sf.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02475; CobW; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cobalamin biosynthesis; Nucleotide-binding;
KW   Porphyrin biosynthesis.
FT   CHAIN           1..354
FT                   /note="Protein CobW"
FT                   /id="PRO_0000089999"
FT   DOMAIN          261..354
FT                   /note="CobW C-terminal"
FT   BINDING         18..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         80..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         188..191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  38121 MW;  B6CE32F0CB04889B CRC64;
     MTTARANQGK IPATVITGFL GAGKTTMIRN LLQNADGKRI GLIINEFGDL GVDGDVLKGC
     GAEACTEDDI IELTNGCICC TVADDFIPTM TKLLERENRP DHIIIETSGL ALPQPLIAAF
     NWPDIRSEVT VDGVVTVVDS AAVAAGRFAD DHDKVDALRV EDDNLDHESP IEELFEDQLT
     AADLIVLNKT DLIDASGLKA VRDEVSSRTS RKPTMIEAKN GEVAAAILLG LGVGTESDIA
     NRKSHHEMEH EAGEEHDHDE FDSFVVELGS IADPAAFIDR LKGVIAEHDV LRLKGFADVP
     GKPMRLLIQA VGARIDQYYD RAWGAGEKRG TRLVVIGLHD MDEAAVRAAI TALV