ID   COBQ_LISMH              Reviewed;         511 AA.
AC   B8D9Y4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-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=LMHCC_1443;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK39788.1; -; Genomic_DNA.
DR   RefSeq; WP_012581506.1; NC_011660.1.
DR   AlphaFoldDB; B8D9Y4; -.
DR   SMR; B8D9Y4; -.
DR   KEGG; lmh:LMHCC_1443; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
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_1000116907"
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;  56277 MW;  5247C7F984662361 CRC64;
     MVKQIMIQGT ASDAGKSVLV AGLCRLFKNK GKQVVPFKSQ NMSLNSFITV TGDEMGRAQV
     FQAEAAGVFP DVRMNPVLLK PTNDRQSQVI FMGAILDNMD AVTYHDFKQT LIPKIQAVYQ
     SLADENDIIV LEGAGSPAEI NLNDRDIVNM GMAKMVDAPV VLVADIDKGG VFASIYGTIM
     LLNEEERARI KGVIINKFRG DVALLQPGID MIEELTNVPV IGVIPYANLQ LEEEDSVSLS
     GKNYAPDSNA LLDIAIICLP RISNFTDFHS LEIQPEISLR YIRNLADFGK PDLVIIPGSK
     NTLEDMAFLE ESGLKKAIQN FAENAGKVIG ICGGYQMLGQ KMLDPNQVES RQLEIAGLGL
     LDTETIFLEQ KRTTQITGVT HSGEAVEGYE IHMGETKRGE STSPFCKIKA VNGNEETHQD
     GAISANKNII GTYIHGIFDN DVFLGNLFDE LLTRKNQSIY PHEIINLKEH KEQEYDKLAA
     LLEANIQMDQ LEKIMKGEKI CVSTQKPAIK E