ID   COBQ_PROMT              Reviewed;         504 AA.
AC   Q46JR6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PMN2A_0771;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000095; AAZ58262.1; -; Genomic_DNA.
DR   RefSeq; WP_011294859.1; NC_007335.2.
DR   AlphaFoldDB; Q46JR6; -.
DR   SMR; Q46JR6; -.
DR   STRING; 59920.PMN2A_0771; -.
DR   EnsemblBacteria; AAZ58262; AAZ58262; PMN2A_0771.
DR   KEGG; pmn:PMN2A_0771; -.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   PhylomeDB; Q46JR6; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002535; 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; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332365"
FT   DOMAIN          258..454
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   504 AA;  56581 MW;  F8823F468B8DCEAF CRC64;
     MNIDLKRTPL MVLGTSSGAG KTLIATAICR CLKRKGEQPI PFKGQNMSNN AWVDTKGREM
     AYSQALQSWS AGLEPSAEMN PVLLKPKGDC TSEVIHLGKS VGTSRAINYY EDWFDSGWEA
     IKKGLAILLK SKTDGRLILE GAGSPVEVNL QHKDLTNLKL AKYLNANCIL VADIERGGVF
     AQIIGTIALM KPDEKKLIKG IIINRFRGDK ALFETGVTWI EKETGIPVLG ILPWLKEIFP
     PEDSLDLLER KQINQGAEIE IAIIKLPRIS NFSDLDPFFS DSSIQMRWIE PGQELGEPDV
     LIIPGSKQTI KDLESLNKTG LSNQIKNYAK KGGNIFGICG GLQMLGKSLE DPHQQESINE
     TSTSSNMGMN LLPIKTTFRE IKHTSQREEK VSWPFSQNIK GFEMHYGESD LINNKDSEII
     SLFKNSSLGW VIEKKDKSFV GGTYLHGIFE NDEWRRQWIN KIRQKKGLNH LKIDEENNSD
     KRERLLDLLT DAFEKNINID ILIK