ID   COBQ_PHOLL              Reviewed;         512 AA.
AC   Q7N2T7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=plu2987;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571869; CAE15361.1; -; Genomic_DNA.
DR   RefSeq; WP_011147206.1; NC_005126.1.
DR   AlphaFoldDB; Q7N2T7; -.
DR   STRING; 243265.plu2987; -.
DR   EnsemblBacteria; CAE15361; CAE15361; plu2987.
DR   GeneID; 24170197; -.
DR   KEGG; plu:plu2987; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   BioCyc; PLUM243265:PLU_RS14855-MON; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002514; 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; Reference proteome.
FT   CHAIN           1..512
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141314"
FT   DOMAIN          251..451
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        443
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   512 AA;  55665 MW;  184C2404AEFB4070 CRC64;
     MGLSLMLQGT ASDVGKSVLV AGLCRIFVQD GYRCAPFKSQ NMALNSGITI NGEEMGRAQI
     FQAEAAGIEP DVRMNPVLLK PTSERKAQVV LMGKVACSMN AVEYHQYKPS LQQQICEVFH
     SLASEYDVIV LEGAGSPAEI NLRDRDIVNM GMAEMVDAPV LLVADIDRGG VFAAIYGTLA
     LLRPAEKARV KGVIINKFRG DISLLQPGIE QIEALTGVPV LGVMPWLDID LEDEDGVALQ
     TGKYDGATEK ALDITVIRLP HIANFTDFNA LAVQPDVRLR YVTQPSALQP SDLIILPGSK
     NTLGDLQWLR QNGLADALLT AHQAGVPVIG ICGGYQMLGK RIIDGVESGI EQMDGLGLLD
     METRFAHEKV TTRVNGNCLL ALPGLLSECV EQPIRGYEIH MGSSLLGADA TPFIDITERN
     GQSGGWCDGA VNREGSVMGS YIHGLFDSAN FTRALLNALR QRKGLAAYQG EILDYTHYKQ
     TQFDLLAKAM REHLDIERIY QCMKTHRQGS VP