ID   COBQ_METPP              Reviewed;         508 AA.
AC   A2SI71;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mpe_A2304;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(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; CP000555; ABM95260.1; -; Genomic_DNA.
DR   RefSeq; WP_011829897.1; NC_008825.1.
DR   AlphaFoldDB; A2SI71; -.
DR   STRING; 420662.Mpe_A2304; -.
DR   EnsemblBacteria; ABM95260; ABM95260; Mpe_A2304.
DR   KEGG; mpt:Mpe_A2304; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_1_4; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000366; 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..508
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332346"
FT   DOMAIN          266..464
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        347
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   508 AA;  54594 MW;  D573BD4EC34EF19A CRC64;
     MNGRTRSPAR AVMVLGTTSG AGKSWLATAL CRWYARQGLK VAPFKAQNMS NNARVVPGSG
     GRLGEIGSAQ YFQALAARVL PDVRMNPVLL KPENDTGSQV VVLGEVRADL AAVPWRERSE
     RLWPFAQDAL LALMAENDVV VIEGAGSPAE INLHASDYVN MRTAQAARAA CLLVSDIDRG
     GAFAHLYGTH QLLPAAERAL LRGYVLNRFR GDARLLEPGP QQLLALTGVP TLAVLPMWRG
     HGLPEEDGLH DEGPGWQRGA GNAAASLRIA VVAYPRISNL DEFQPLRQLR GVQLRWARSA
     EELAGADWIV LPGSKHTSGD LAWLREQRID AALARHAAAR RPVLGLCGGL QMLGEALVDP
     HGVEGENGEG NAPGLGLLPL VTAFEPDKLL RRTDACFDGV GDEWSMLRGV QFGGYEIRHG
     RSVQHPALPA AAVALRNAEG EAIGWQQGSV LGLYAHGLFE STEVLRALFG ARVRGLESVF
     DGLADFIDRH FEPGALMRLL ADAEPGKD