ID A0A087RYF3_9ARCH Unreviewed; 279 AA.
AC A0A087RYF3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000256|ARBA:ARBA00014921, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN ECO:0000313|EMBL:KFM18507.1};
GN ORFNames=AAA799P11_01077 {ECO:0000313|EMBL:KFM18507.1};
OS Marine Group I thaumarchaeote SCGC AAA799-P11.
OC Archaea; Nitrososphaerota; Marine Group I.
OX NCBI_TaxID=1502295 {ECO:0000313|EMBL:KFM18507.1, ECO:0000313|Proteomes:UP000029387};
RN [1] {ECO:0000313|EMBL:KFM18507.1, ECO:0000313|Proteomes:UP000029387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AAA799-P11 {ECO:0000313|EMBL:KFM18507.1};
RA Ngugi D.K., Blom J., Alam I., Rashid M., Baalawi W., Zhang G., Hikmawan T.,
RA Guan Y., Antunes A., Siam R., El-Dorry H., Bajic V., Stingl U.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000256|ARBA:ARBA00025166, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFM18507.1}.
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DR EMBL; JOSZ01000017; KFM18507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087RYF3; -.
DR PATRIC; fig|1502295.3.peg.1039; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000029387; Unassembled WGS sequence.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00028};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00028}; Ligase {ECO:0000313|EMBL:KFM18507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029387}.
FT DOMAIN 4..228
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 279 AA; 31021 MW; 9A252ED10D11155C CRC64;
MKSLMIQGTS SGAGKSTLVA ALCRIFEQKG YLVAPFKSQN MSNFGYATPD FEISRAQAIQ
AIAAKCPIEP DLNPIMLKPL GNYYSAVYLN GKYYKKMHAK DYYAKFVKSK GIKAATTSLS
KLQKNYDLVI LEGAGSPAEI NLQKYDIANM QIAQKANASV LLVSDIDRGG SFASLIGTMA
LIERKYKKLV KGFVLNKFRG DVDVLKPGFR KIKQLTKIPI LGTIPMTKID LPEEDSLHVK
AKQMRWTKNN ISKIDKELDK LAKTVKNNLD IKAIEEMIK
//