ID   COBQ_RHOCA              Reviewed;         483 AA.
AC   P0CY57; O68093; Q52686;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Cobyric acid synthase;
GN   Name=cobQ;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=7635831; DOI=10.1128/jb.177.15.4481-4487.1995;
RA   Pollich M., Klug G.;
RT   "Identification and sequence analysis of genes involved in late steps in
RT   cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus.";
RL   J. Bacteriol. 177:4481-4487(1995).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000305}.
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; Z46611; CAA86584.1; -; Genomic_DNA.
DR   PIR; S52226; S52226.
DR   AlphaFoldDB; P0CY57; -.
DR   UniPathway; UPA00148; -.
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; 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; 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..483
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141327"
FT   DOMAIN          248..437
FT                   /note="GATase cobBQ-type"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   483 AA;  50410 MW;  000B7D4DD466130B CRC64;
     MTALMIQGAG SNVGKSMLVA GLCRAARRRG LTVAPFKPQN MSNNAAVTAD GGEIGRAQAL
     QALACGLEPV TDMNPILLKP ESDVGAQVVV QGKRLTTTRA RDYATLKPQL MGAVLESFNR
     LKATHDLVIV EGAGSPAEVN LRAGDIANMG FARAADVPVV LVGDIDRGGV IAQIVGTQAV
     LDPADAEMIS GFLINKFRGD VTLFDDGYRL IGARTGWRGF GTLPWFPLAH KLPAEDALDI
     ASGPATGGTV IACLTLSRIA NFDDLDPLAA EPGVRMVMVQ PGQPIPAEAR LVILPGSKST
     RGDLAFLREQ GWDIDLAAHV RRGGHVLGIC GGYQMLGRSV ADPEGIEGPA GTTPGLGLLD
     VETVMTPDKR LTRVRVRATH AGSGLAVEGY EIHIGRTEGA DRARPFAIVE GQNEGAMSAD
     GRVIGSYLHG LFGADAFRAA FLRGLGIRAS GQSHAAGVEA ALDALADHLE THLDVTGILA
     LAR