COBQ_RHIE6
ID COBQ_RHIE6 Reviewed; 484 AA.
AC B3PQX7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=RHECIAT_CH0002598;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001074; ACE91550.1; -; Genomic_DNA.
DR RefSeq; WP_012484157.1; NC_010994.1.
DR AlphaFoldDB; B3PQX7; -.
DR SMR; B3PQX7; -.
DR EnsemblBacteria; ACE91550; ACE91550; RHECIAT_CH0002598.
DR GeneID; 45957882; -.
DR KEGG; rec:RHECIAT_CH0002598; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_0_5; -.
DR OMA; DVRMNPL; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008817; 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_1000090241"
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; 51168 MW; E7DDA39695308E5B CRC64;
MARAIMLQGT GSDVGKTVLV AGLCRLAANR GLTVRPFKPQ NMSNNAAVAD DGGEIGRAQW
LQSLAARTPS SVHMNPVLLK PQSENGSQII VQGRVFGQAK GRDYQRLKPQ LLGAVLASFE
KVADGADLVI VEGAGSPAEI NLRAGDIANM GFATQAGVPV VLVGDIDRGG VIASLVGTHA
ILADADRAMI SGYIINKFRG DVSLFDNGIR AIEGFTGWPC FGVVPWLSGA ARLPAEDSVV
LERLAKGGGG ALKIAVPVLP RIANFDDLDP LRAEPDVELV FIRSGERLPA DASLVVLPGS
KSTISDLADL RAAGWDRDLF AHVRRGGRVI GICGGYQMLG RTVHDPLGLE GGTLETPGLA
LLDVETEMAP EKTVRNSHAR STEYDAPLAG YQIHLGMTRG PDCGRPSAIV DGVPDGALSA
NGLIMGTYLH GLFASDAYRT RLLQSFGLSG ERRNYRESVD KALDEIAGEL ERYLDPRWLA
GLVG
