ID   A0A2P8HL20_9BACI        Unreviewed;       490 AA.
AC   A0A2P8HL20;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=B0H94_10562 {ECO:0000313|EMBL:PSL46912.1};
OS   Salsuginibacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salsuginibacillus.
OX   NCBI_TaxID=517424 {ECO:0000313|EMBL:PSL46912.1, ECO:0000313|Proteomes:UP000242310};
RN   [1] {ECO:0000313|EMBL:PSL46912.1, ECO:0000313|Proteomes:UP000242310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.07653 {ECO:0000313|EMBL:PSL46912.1,
RC   ECO:0000313|Proteomes:UP000242310};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2018) 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}.
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:PSL46912.1}.
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DR   EMBL; PYAV01000005; PSL46912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8HL20; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000242310; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242310}.
FT   DOMAIN          1..230
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          249..434
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   490 AA;  53306 MW;  285940DC4A981F32 CRC64;
     MIQGTHSDAG KSVIVTALCR IFAEDGWHTA PFKSQNMALN SYVTAAGEEI GRAQGVQAEA
     AGIEPTTDMN PILLKPTGGT GAQVVLHGKP YENMSAGSYR KDFFETGLEV IHNAYNRLAE
     SYDAVVIEGA GSPAEINLND RELVNMRVAN IARAPVILVG DIEKGGVFAS LVGTLQLLEA
     QDRAKVKGVM INKFRGDVSL LEPGIDWFEA YTGIPVLGII PYEDLTVEAE DSVALDRYTS
     AANETKELDI AVIRHPHLAN FTDIDPFFEE PDCHVRMVQH PEELGIPDML LIPGSKSTLH
     DLAVMKEAGL FAAIGRLKAC GTRIVGICGG YQMLGLELLD EQQLESKVAT SAGLGLLPIS
     TTIAEDKTTI RTTGNLTFKG SEHEVSGYEI HMGVTKHTSE TDALLETTSG QDGAKDQAEQ
     VIGTYLHGLF HNDAFREYFL NDIRETKGLA PIYGRSSYQA RRESGFDQAA DLVRRNCRMD
     AIYALMDEEK
//