ID   COBQ_PSEU2              Reviewed;         486 AA.
AC   Q4ZQ64;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Psyr_3676;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY38708.1; -; Genomic_DNA.
DR   RefSeq; WP_003404269.1; NC_007005.1.
DR   RefSeq; YP_236746.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZQ64; -.
DR   SMR; Q4ZQ64; -.
DR   STRING; 205918.Psyr_3676; -.
DR   EnsemblBacteria; AAY38708; AAY38708; Psyr_3676.
DR   KEGG; psb:Psyr_3676; -.
DR   PATRIC; fig|205918.7.peg.3777; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; GREVHDP; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000426; 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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
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; PF01656; CbiA; 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..486
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332377"
FT   DOMAIN          248..435
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        329
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   486 AA;  52168 MW;  47B6225B34F932A2 CRC64;
     MSTLMVQGTT SDAGKSTLVT ALCRWLTRQG VKVVPFKPQN MALNSAVTAD GGEIGRAQAV
     QAQACYLEPH TDMNPVLLKP NSDTGAQVII HGRAVTTMNA VAYHGYKEIA MQAVLESHRR
     LGESYPVIVV EGAGSPAEIN LRANDIANMG FAEAVDCPVL LIADINRGGV FAHLVGTLEL
     LSLSEQARVK GFIINRFRGD IALLQPGLDW LEARTGKPVV GVLPYVMDLH LEAEDGLDQR
     QTDKVEHVLN VVVPVLPRIS NHTDFDPLRL HPQVNLQFIG PGKAIPPADL IILPGSKSVR
     SDLNYLRNNG WDTAIARHLR YGGKLMGICG GLQMLGEQVH DPLGLEGAAG SSAGFGLLAM
     STVLEAEKQL RNVRGRLTLE DAEVSGYEIH AGVTTGPALE QAAVQLDDGR CDGAQSADGQ
     VLGTYLHGLF ESPAACSALL RWAGLANVQS VDYHALRERD IERLADLVEK HLDGPLLREL
     CGLEAN