ID J7L838_NOCAA Unreviewed; 511 AA.
AC J7L838;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:AFR07570.1};
GN OrderedLocusNames=B005_0625 {ECO:0000313|EMBL:AFR07570.1};
OS Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR07570.1, ECO:0000313|Proteomes:UP000003779};
RN [1] {ECO:0000313|EMBL:AFR07570.1, ECO:0000313|Proteomes:UP000003779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX PubMed=23105086; DOI=10.1128/JB.01522-12;
RA Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT Associated with Honeybees.";
RL J. Bacteriol. 194:6358-6359(2012).
RN [2] {ECO:0000313|Proteomes:UP000003779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT with honeybees.";
RL Submitted (AUG-2012) 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|PROSITE-ProRule:PRU00605}.
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DR EMBL; CP003788; AFR07570.1; -; Genomic_DNA.
DR RefSeq; WP_014910032.1; NC_018524.1.
DR AlphaFoldDB; J7L838; -.
DR STRING; 1205910.B005_0625; -.
DR KEGG; nal:B005_0625; -.
DR PATRIC; fig|1205910.3.peg.586; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_11; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000003779; Chromosome.
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 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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:AFR07570.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003779}.
FT DOMAIN 15..244
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 265..438
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 489..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 432
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 511 AA; 53917 MW; 9473F8FFEBB5CA1F CRC64;
MSGNGTGRVG ASGLLVAGAT SDAGKSVVTT ALCRAFARRG IRVAPYKAQN MSNNSMVCHG
SDGRPAEIGR AQWVQALAAR ALPEPAMNPV LLKPGSDRRS HAVLLGHPAG EVSSSNWEEG
RRHLAEAAHA AFDDLASRYD VVVAEGAGSP TEINLRAGDY VNMGLARHAG LPTVVVGDID
RGGVFAALYG TVALLEPADQ ELIAGFVINR FRGDPELLRP GLEDLERLTG RRVYGTLPWD
SRLWLDSEDA LDLEGRRADG VSARRVAVVR LPRISNFTDV DALGLEPGLD VVFASGPRDI
ADADLVVLPG TRSTLADLAW LRSRGLDAAI VEHARRGRPV LGVCGGFQML GRDVHDPEGV
EAEPGAYAEG LGLLDVRTDF TPDKTLRLPS GEALGAPVDG YEIHHGRITV GDGVEAFPGG
ARSGVVFGTM WHGALEGDAF RSAFLAETLD QEPSGVDFPA ARERRVDLLA DLVERYLDVD
ALLELARSGG SEPMPVLAPG GPPARTAGSA R
//
