COBQ_RHIEC
ID COBQ_RHIEC Reviewed; 484 AA.
AC Q2K7B5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=RHE_CH02494;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(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; CP000133; ABC91271.1; -; Genomic_DNA.
DR RefSeq; WP_011425749.1; NC_007761.1.
DR AlphaFoldDB; Q2K7B5; -.
DR SMR; Q2K7B5; -.
DR STRING; 347834.RHE_CH02494; -.
DR EnsemblBacteria; ABC91271; ABC91271; RHE_CH02494.
DR KEGG; ret:RHE_CH02494; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_0_5; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001936; 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; 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..484
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002373"
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; 51349 MW; E9DE6343C09C995D CRC64;
MARTIMLQGT GSDVGKTVLV AGLCRLAANA GLTVRPFKPQ NMSNNAAVAD DGGEIGRAQW
LQSMAARTPS SVHMNPVLLK PQSENGSQII VQGRVFGQAK GRDYQRLKPQ LLGAVLESFE
NVCAGADLVV VEGAGSPAEI NLRTGDIANM GFATKAGVPV VLVGDINRGG VIASLVGTQA
ILDEGDRAMI AGYLINKFRG DVSLFDDGIR AIEGFTGWPC FGVVPWLQAA TRLPAEDSVV
LERLARSGTG ALKIAVPMLP RIANFDDLDP LRAEADVELV FVRGGERLPA DASLVILPGS
KSTISDLADL RVQGWDRDLA AHVRRGGRVI GICGGYQMLG RTVRDPLGIE GGRIEAAGLA
LLDVETEMAP EKTVRNSQAR SSEYDVSLAG YQIHLGVTRG PDCVRPSAII DGAPDGALSA
DGRIMGTYLH GLFGSDAYRA RLLQSFGLSG ERRNYRDSVE QALDEIAGEL ERHLDPHWLA
GLLG