ID   A0A1I6RHS3_9BACL        Unreviewed;       496 AA.
AC   A0A1I6RHS3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=SAMN05444972_105103 {ECO:0000313|EMBL:SFS64291.1};
OS   Marininema halotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Marininema.
OX   NCBI_TaxID=1155944 {ECO:0000313|EMBL:SFS64291.1, ECO:0000313|Proteomes:UP000198660};
RN   [1] {ECO:0000313|EMBL:SFS64291.1, ECO:0000313|Proteomes:UP000198660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45789 {ECO:0000313|EMBL:SFS64291.1,
RC   ECO:0000313|Proteomes:UP000198660};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FPAA01000005; SFS64291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6RHS3; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000198660; Unassembled WGS sequence.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; 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; cd05389; CobQ_N; 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; 1.
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; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 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; 1.
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}.
FT   DOMAIN          4..228
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          252..440
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   496 AA;  54597 MW;  3225A684459AE6CA CRC64;
     MRGIMIQGTA SDVGKSVVAT AFCRLFAEEG YRVAPFKAQN MALNSFVTVK GGEIGRSQAV
     QAEAAGIEAT VDMNPILLKP KGERIAEVIV HGQHYADLEA GEYQNRTISE MLGPVSQSLH
     RLAEQVDVLI IEGAGSPAEI NLKERDIVNM RTAALADVPV ILVADIDRGG VFASVVGTLE
     ILDPSERERI KGIVINKFRG DVSLLQPGLD WLEEKTGIPV LGVLPWKKVE IDPEDSLSLD
     KIVTHPSEKA IDIALIRFPH ISNFTDFMPL MRIPGVGVRW IENDTDWGNP DVVILPGTKN
     TMADLKWLYQ KGLADRIQQV ASTHGFVVGI CGGFQMLGHC LVDPEGVESD IPHADGLGLL
     PVNIHFERRK RTVQTKGVVN STLWGEEIQV VGYEIHRGRS QYNGEAVPFL YQNDGEVDGA
     VVAEGRIWGT HLHGVFDQPA FLRRWIEELR GKKNLPSLGE NDFPISSKES SYSELAQWVR
     DHLDMKKVQA MLEGKG
//