COBQ_CLOB6
ID COBQ_CLOB6 Reviewed; 493 AA.
AC C3L2K4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CLJ_B0964;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-2008) 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:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CP001083; ACQ53069.1; -; Genomic_DNA.
DR RefSeq; WP_012720839.1; NC_012658.1.
DR AlphaFoldDB; C3L2K4; -.
DR SMR; C3L2K4; -.
DR EnsemblBacteria; ACQ53069; ACQ53069; CLJ_B0964.
DR KEGG; cbi:CLJ_B0964; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002333; Chromosome.
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-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase.
FT CHAIN 1..493
FT /note="Cobyric acid synthase"
FT /id="PRO_1000201966"
FT DOMAIN 246..440
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 326
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 432
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 493 AA; 55310 MW; 2951B2AFB80AFC57 CRC64;
MAKIMIQGTA SSVGKSLIVA ALCRIFKQDG YSVCPFKSQN MSLNSYITLD GKEMGRAQVL
QAYAAGLEPE VYMNPILLKP TSDKKSQIIV NGKVYGNSTA MEYHNLKIKF KGMLKEQFKK
LEEDFDIVVM EGAGSPAEIN LRDRDIVNMG MAEIVDAPVL LVGDIDKGGV FASLAGTMLL
LNEGEKERVK GTIINKFRGD VEILNPGLDM LEDIIHIPCL GVVPYTRLQL EDEDGAVEFN
KKAYAPIDIA VIKMPHISNF TDLDALKSEE DVSIRFITSK EEFKEPDLLV IPGSKNTIED
LLYLRKCGLE ESIKEYSKDG KIIGICGGYQ VLGSKIKDPY KVETDLGEIE GLNLLDMETT
FEKEKITTRV SAKLINEEIE NIVYGYEIHM GISEYSENVK PLFKIYDKNG EKVDYFDGAI
NEKGNVMGTY IHGVFDGIVF REKIINELRV KKGLKKKKSQ VYEHMREKEL DKLADIVRQS
LDMEKIYSII GMK