ID   COBQ_CERS4              Reviewed;         481 AA.
AC   Q3IZR0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=RHOS4_24060;
GN   ORFNames=RSP_0796;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000143; ABA79974.1; -; Genomic_DNA.
DR   RefSeq; WP_011338494.1; NZ_CP030271.1.
DR   RefSeq; YP_353875.1; NC_007493.2.
DR   AlphaFoldDB; Q3IZR0; -.
DR   SMR; Q3IZR0; -.
DR   STRING; 272943.RSP_0796; -.
DR   PRIDE; Q3IZR0; -.
DR   EnsemblBacteria; ABA79974; ABA79974; RSP_0796.
DR   KEGG; rsp:RSP_0796; -.
DR   PATRIC; fig|272943.9.peg.2755; -.
DR   eggNOG; COG1492; Bacteria.
DR   OMA; EIHHGVA; -.
DR   PhylomeDB; Q3IZR0; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002703; Chromosome 1.
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..481
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332380"
FT   DOMAIN          248..435
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        330
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   481 AA;  50883 MW;  CCEFD43E5DFC806E CRC64;
     MPAVMIQGTG SDVGKSLLVA GLCRAARRRG LSVAPFKPQN MSNNAAVTAD GGEIGRAQAL
     QARASGLEPL TDMNPVLLKP ESDHGSQVIV QGRRVGTLRA RDWFERKPAL MAPVLESFAR
     LTAAHDLVIV EGAGSPAEVN LRRGDIANMG FARTAGVPVV LAGDIDRGGV IAQLVGTQAV
     IDPEDAAMIA GFLVNKFRGD VRLFDEGYRL IEARTGWRGY GVVPFFPEAA LLPAEDALDL
     GRPTGQGALT VAWLAFSRVA NFDDLDPLKQ EPGLTVRMVR PGQPIPAEAD LVILPGTKST
     RGDLAFLRAQ GWDVDLRAHH RRGGRVLGIC GGYQMLGRSV ADPEGLEGAP GVTEGLGLLD
     VETVMHPDKR LTRVAGRHRA SGAELTGYEI HIGATEGPDC ARPFAEIEGR PEGATSADGR
     VVGSYLHGMF GADGFRRAFL ESLGAATSDL AYDARVETVL DALADHLETH VDVAGLLALA
     R