ID   COBQ_LISMC              Reviewed;         511 AA.
AC   C1L2B3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Lm4b_01212;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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; FM242711; CAS04979.1; -; Genomic_DNA.
DR   RefSeq; WP_012681258.1; NC_012488.1.
DR   AlphaFoldDB; C1L2B3; -.
DR   SMR; C1L2B3; -.
DR   KEGG; lmc:Lm4b_01212; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   BioCyc; LMON568819:LM4B_RS06050-MON; -.
DR   UniPathway; UPA00148; -.
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..511
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000201969"
FT   DOMAIN          251..443
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   511 AA;  56163 MW;  F69A5CFDC54A1965 CRC64;
     MVKQIMIQGT ASDAGKSVLV AGLCRLFKNK GKRVVPFKSQ NMSLNSFITA TGDEMGRAQV
     FQAEAAGVFP DVRMNPVLLK PTNDRQSQVI FMGAILDNMD AVTYHDFKQT LIPKIQAVYQ
     SLADENDIIV LEGAGSPAEI NLNDRDIVNM GMAKMVDAPV VLVADIDKGG VFASIYGTIM
     LLNEEERARI KGVIINKFRG DVALLQPGID MIEELTNVPV IGVIPYANLQ LEEEDSVSLS
     GKNYVPDSNA LLDIAIICLP RISNFTDFHI LEIQPDISVR YIRNIADFGN PDLVIIPGSK
     NTLEDMAFLE ESGLKNAIQN YAKNAGKVIG ICGGYQMLGK KMLDPNQVES KQLEIAGLGL
     LDTETIFLDQ KRTTQITGVT HSGEAVEGYE IHMGETKRGE STSPFCEIKA VNGNEETHQD
     GAISVNKNII GTYIHGIFDN DVFLGNLFDE LLTGKNKSVY PHEIINLKEH KEQEYDKLAA
     LLEANIQMDQ LEKIMKGEKI CVSTQKPAIK E