ID M0JTF6_9EURY Unreviewed; 323 AA.
AC M0JTF6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Cobalamin biosynthesis protein CbiG {ECO:0000313|EMBL:EMA12266.1};
DE SubName: Full=Cobalt-precorrin 5A hydrolase {ECO:0000313|EMBL:QUJ71488.1};
DE EC=3.7.1.12 {ECO:0000313|EMBL:QUJ71488.1};
GN Name=cbiG {ECO:0000313|EMBL:QUJ71488.1};
GN ORFNames=C436_15649 {ECO:0000313|EMBL:EMA12266.1}, KDQ40_12345
GN {ECO:0000313|EMBL:QUJ71488.1};
OS Haloarcula sinaiiensis ATCC 33800.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA12266.1, ECO:0000313|Proteomes:UP000011659};
RN [1] {ECO:0000313|EMBL:EMA12266.1, ECO:0000313|Proteomes:UP000011659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA12266.1,
RC ECO:0000313|Proteomes:UP000011659};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [2] {ECO:0000313|EMBL:QUJ71488.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ71488.1};
RA Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT Haloarcula sinaiiensis.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AOLR01000023; EMA12266.1; -; Genomic_DNA.
DR EMBL; CP073366; QUJ71488.1; -; Genomic_DNA.
DR RefSeq; WP_004964946.1; NZ_CP073366.1.
DR AlphaFoldDB; M0JTF6; -.
DR GeneID; 64823759; -.
DR KEGG; hsin:KDQ40_12345; -.
DR PATRIC; fig|662476.7.peg.3135; -.
DR OrthoDB; 4722at2157; -.
DR Proteomes; UP000011659; Unassembled WGS sequence.
DR Proteomes; UP000682967; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.11220; -; 1.
DR Gene3D; 3.30.420.180; CobE/GbiG C-terminal domain; 1.
DR InterPro; IPR021744; CbiG_N.
DR InterPro; IPR002750; CobE/GbiG_C.
DR InterPro; IPR036518; CobE/GbiG_C_sf.
DR InterPro; IPR038029; GbiG_N_sf.
DR PANTHER; PTHR37477; COBALT-PRECORRIN-5A HYDROLASE; 1.
DR PANTHER; PTHR37477:SF1; COBALT-PRECORRIN-5A HYDROLASE; 1.
DR Pfam; PF01890; CbiG_C; 1.
DR Pfam; PF11760; CbiG_N; 1.
DR SUPFAM; SSF159672; CbiG N-terminal domain-like; 1.
DR SUPFAM; SSF159664; CobE/GbiG C-terminal domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:QUJ71488.1}.
FT DOMAIN 62..140
FT /note="Cobalamin synthesis G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11760"
FT DOMAIN 205..321
FT /note="CobE/GbiG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01890"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 34483 MW; 161D33F444E16CD2 CRC64;
MSTDTDDDSG SHGCKAPDSD GEVAENIAIV AFERKMDTAE DIVDGIGDRY ESIDILEYHG
DVFEEYWGEY DCFIGLMASG IAMRKTAHLL DDKWDDPAIC VVDEELTWAI PITGGHHGAN
QVADDLASMG AVPAMTTASE AADKQGVEKQ AKALDAHVVN GDSTVATNLA VLDDELGPIE
RLDGPKAVLV DDDVTVLKRN KDDGVVLGCG SVAGADVEQF HAAWEQALDE ADLDRDDVEF
VATGTRKADE EGMLAAAEEW GLGVIAFEKE TLEEFEGPTP SRSKELIGWP GIAEASAIAA
GSEHDLLAEK TRYDEAVTVA IGR
//
