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