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COBQ_RHIL3
ID   COBQ_RHIL3              Reviewed;         488 AA.
AC   Q1MFE8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=RL2836;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK08326.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1MFE8; -.
DR   SMR; Q1MFE8; -.
DR   STRING; 216596.RL2836; -.
DR   EnsemblBacteria; CAK08326; CAK08326; RL2836.
DR   KEGG; rle:RL2836; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_0_5; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000006575; 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; 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..488
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332379"
FT   DOMAIN          255..442
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   488 AA;  51830 MW;  9275D9C1A76231CB CRC64;
     MRATMARAIM LQGTGSDVGK TVLVAGLCRL AANRGLTVRP FKPQNMSNNA AVADDGGEIG
     RAQWLQSLAA RTPSSVQMNP VLLKPQSENG SQIIVQGRVF GQAKGRDYQR LKPELLGAVL
     ESFEKVAAGA DLVIVEGAGS PAEINLRAGD IANMGFATRA GVPVVLVGDI DRGGVIASLV
     GTHAILEDGD RAMIAGYIIN KFRGDVSLFD DGVRAIEGFT GWPCFGIVPW LRGAARLPAE
     DSVVLERLVR GGAGALKIAV PVLPRIANFD DLDPLRSEPD VELVFVRSGE RIPADASLVV
     LPGSKSTISD LADFRAQGWD RDLQAHVRRG GRVIGICGGY QMLGRMVHDP LGIEGGTLET
     PGLGLLDIET EMAPEKTVRN SQARSTEYDA PLAGYQIHLG VTRGPDCDRP SAIIDGASDG
     ALSADGRIMG TYLHGLFGSD AYRAGLLQSF GLSGERRNYR ESVEQALDEI AGELERHLDP
     RWLAGLLG
 
 
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