ID F6DJR6_THETG Unreviewed; 672 AA.
AC F6DJR6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Ththe16_2303 {ECO:0000313|EMBL:AEG34663.1};
OS Thermus thermophilus (strain SG0.5JP17-16).
OG Plasmid pTHTHE1601 {ECO:0000313|EMBL:AEG34663.1,
OG ECO:0000313|Proteomes:UP000009233}.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=762633 {ECO:0000313|EMBL:AEG34663.1, ECO:0000313|Proteomes:UP000009233};
RN [1] {ECO:0000313|Proteomes:UP000009233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0.5JP17-16 {ECO:0000313|Proteomes:UP000009233};
RC PLASMID=Plasmid pTHTHE1601 {ECO:0000313|Proteomes:UP000009233};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA Gladden J., Woyke T.;
RT "Complete sequence of plasmid of Thermus thermophilus SG0.5JP17-16.";
RL Submitted (MAY-2011) 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|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|HAMAP-Rule:MF_00028}.
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DR EMBL; CP002778; AEG34663.1; -; Genomic_DNA.
DR RefSeq; WP_014511278.1; NC_017273.1.
DR AlphaFoldDB; F6DJR6; -.
DR KEGG; tts:Ththe16_2303; -.
DR PATRIC; fig|762633.3.peg.2305; -.
DR HOGENOM; CLU_019250_2_1_0; -.
DR UniPathway; UPA00148; UER00236.
DR Proteomes; UP000009233; Plasmid pTHTHE1601.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043752; F:adenosylcobinamide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00544; CobU; 1.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR003203; CobU/CobP.
DR InterPro; IPR011698; GATase_3.
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 Pfam; PF02283; CobU; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51274; GATASE_COBBQ; 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};
KW Nucleotidyltransferase {ECO:0000313|EMBL:AEG34663.1};
KW Plasmid {ECO:0000313|EMBL:AEG34663.1};
KW Transferase {ECO:0000313|EMBL:AEG34663.1}.
FT DOMAIN 8..225
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 247..393
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 463..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 410
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 672 AA; 72928 MW; 1BB88A54C4B6EB08 CRC64;
MGRAKALIVW GTGSGVGKSL FAAGLLRHFK RLGLKAAPFK AQNMANHARV VQGGEIASAQ
WLQALAAGVE PEVRMNPVLV KPFGERGAQV VVWGKVDPFL SRLPWRERKL HLEAPVREAL
EGLLAEYELL VLEGAGSPVE RNLWPDLPNL KVAEWADAKA LLVADVDQGG ALGALYGTWA
LLGEHRKRLI GFAFNKFRGD LELLKPAYAL LRDWTGLPVL GTLPLLPLAL PEEDGFRYRQ
PAGNGPKVAL LRYPHAANLD EFWPLSELAQ VVYAHSPEEA EGAWLLILPG SRLPARDLPW
LQAFLPLIQR HLEAGKPVLA VCGGAEMLSE ALLDEEGVEE RGHFPGLGLL PYRVRMAREK
TVERRRVRLQ GLSGYWGRLE GLEVEGYEIH HGQGLPLFHQ EGPLLATWLH GLLENPGVQK
ALFGGEARGL EEGLEALADA LEAHLDLRAL HRALGLTGRA FPASPAGAKA SAEHPDPPPP
PGLVLLLGGA KSGKSRLAQR LAGPFATLVA TAEARDEEMA ERIRRHQEER PPTWETLEEP
LDLPGALKRA RHPTVVVDCL TLWVANLMER GLDPLLEARR FLSAVEESGK RVIAVSNEVG
MGIVPQNPLA RRYRDLLGQV NALLAEAAQE AYLLVAGRAL PLGGGKVPAQ EAKRPGSHGG
EPGPGRSRDP GP
//
