COBQ_RHILW
ID COBQ_RHILW Reviewed; 484 AA.
AC B5ZT17;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Rleg2_2137;
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304;
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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; CP001191; ACI55420.1; -; Genomic_DNA.
DR RefSeq; WP_012557973.1; NC_011369.1.
DR AlphaFoldDB; B5ZT17; -.
DR SMR; B5ZT17; -.
DR STRING; 395492.Rleg2_2137; -.
DR EnsemblBacteria; ACI55420; ACI55420; Rleg2_2137.
DR KEGG; rlt:Rleg2_2137; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_0_5; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008330; 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..484
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090242"
FT DOMAIN 251..438
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 430
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 484 AA; 51614 MW; 3E6F902A80895516 CRC64;
MARAIMLQGT GSDVGKTVLV AGLCRLAANR GLAVRPFKPQ NMSNNAAVAD DGGEIGRAQW
LQSLAARAPS SVHMNPVLLK PQSENGSQII VQGRVFGQSK GRDYQRLKPQ LLGAVLESFE
KVAAGADLVI VEGAGSPAEI NLRAGDIANM GFATRAGVPV VLVGDIDRGG VIASLVGTHA
ILDDGDRAMI AGYIINKFRG DISLFDDGIR AIEGFTGWPC FGVVPWLPGA ARLPAEDSVV
LERLAKGRAG ALKIAVPVLP RIANFDDLDP LRAEPDVELV FVRSGERLPA DASLVILPGS
KSTISDLADF RAEGWDRDLH MHVRRGGRVI GICGGYQMLG RTVRDRLGIE GGTLETPGLA
LLDVETEMAP EKTVRNSHAR STEYDVPLAG YQIHLGITHG PDCDRPSAIV DGVPDGALSA
DGRIVGTYLH GLFGSDAYRT RLLQSFGLSG ERRNYRESVE QALDEIAGEL ERYLDPRWLA
GLLG