ID   COBQ_PROM1              Reviewed;         494 AA.
AC   A2C3V9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=NATL1_16121;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM76169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C3V9; -.
DR   SMR; A2C3V9; -.
DR   STRING; 167555.NATL1_16121; -.
DR   EnsemblBacteria; ABM76169; ABM76169; NATL1_16121.
DR   KEGG; pme:NATL1_16121; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002592; 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..494
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332364"
FT   DOMAIN          248..444
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        436
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   494 AA;  55335 MW;  21D25B0BEEFAF1B1 CRC64;
     MVLGTSSGAG KTLIATAICR CLRRKGEQPI PFKGQNMSNN AWVDTQGREM AYSQALQSWS
     AGLEPSAEMN PVLLKPKGDC TSEVIHLGKS VGTSKAINYY EDWFDSGWEA IKKGLAILLK
     SKIDGRLILE GAGSPVEVNL QHKDLTNLKL AKFLNANCIL VADIERGGVF AQIIGTIALM
     KPDEKKLIKG IIINRFRGDK ALFESGVTWI EKETGIPVLG ILPWLKEIFP PEDSLDLLER
     KQVNKSAEIE IAIIKLPRIS NFSDLDPFFS DSSIQMRWIE PGQDLGNPDV LIIPGSKQTI
     KDLESLNKTG LSNQIKNYAK KGGNIFGICG GLQMLGKTLE DPHKQESIKE QNTFSNMGMN
     LLPIKTTFGE IKHTSQREEK VSWPVSQSLK GFEMHYGESD LINNTDSEII SLFKNSSLGW
     VIEKKDKSFV GGTYLHGIFE NDEWRRQWIN KIRQKKGLNH LKIDKENNND KRERLLDLLT
     DAFEKNINID ILIK