ID   E4LFX8_9FIRM            Unreviewed;       354 AA.
AC   E4LFX8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN   ECO:0000313|EMBL:EFR59354.1};
GN   ORFNames=HMPREF9199_0899 {ECO:0000313|EMBL:EFR59354.1};
OS   Veillonella sp. oral taxon 158 str. F0412.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR59354.1, ECO:0000313|Proteomes:UP000003565};
RN   [1] {ECO:0000313|EMBL:EFR59354.1, ECO:0000313|Proteomes:UP000003565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0412 {ECO:0000313|EMBL:EFR59354.1,
RC   ECO:0000313|Proteomes:UP000003565};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (NOV-2010) 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: 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:EFR59354.1}.
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DR   EMBL; AENU01000020; EFR59354.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4LFX8; -.
DR   STRING; 879309.HMPREF9199_0899; -.
DR   eggNOG; COG1492; Bacteria.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000003565; 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-UniRule.
DR   CDD; cd05389; CobQ_N; 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; 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}; Ligase {ECO:0000313|EMBL:EFR59354.1}.
FT   DOMAIN          5..231
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          254..326
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
SQ   SEQUENCE   354 AA;  39184 MW;  2BBBDF232293FE99 CRC64;
     MAKKIMFQGT SSNVGKSILC TALCRIFYRK GFKTVPFKAQ NMALNSYVTK WGDEIGRAQV
     AQAEAAGIDP IVQMNPVLLK PTGNQSSQVV LMGKPVGVYS AKEYHTKYSL TALDKVKESI
     DFLDSNFDVM VIEGAGSPAE VNLKANDIVN MRIAKMTQAP VYLIADIDRG GAIASIVGTL
     ELLEPEERDL IKGIVINKFR GDIKLLEPAL TFIEEKTGKK VVGVIPAIEN LDIDEEDSVA
     LENKRNSGSK EIQVIVMQTP KISNFTDFDA LNYEPDVSVR FVGPGDVIGK PDLIILPGSK
     NTLADLTYLR ETGFAEEIKN WLLKELQLLV FVEATKCWVK PFMIRIIWKG ILRR
//