COBQ_RHOOB
ID COBQ_RHOOB Reviewed; 512 AA.
AC C1B2W9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=ROP_66390;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH54886.1; -; Genomic_DNA.
DR RefSeq; WP_015890324.1; NC_012522.1.
DR AlphaFoldDB; C1B2W9; -.
DR SMR; C1B2W9; -.
DR STRING; 632772.ROP_66390; -.
DR EnsemblBacteria; BAH54886; BAH54886; ROP_66390.
DR KEGG; rop:ROP_66390; -.
DR PATRIC; fig|632772.20.peg.6925; -.
DR HOGENOM; CLU_019250_2_2_11; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002212; 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.
FT CHAIN 1..512
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116912"
FT DOMAIN 262..442
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 343
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 512 AA; 53659 MW; 69CA5C508E8B4499 CRC64;
MSESRWRGAL LVAGTTSDAG KSVLVAGLCR MLARRGVRVA PFKAQNMSNN SVVTLDGGEI
GRAQALQAAA CGLEPSVRFN PVLLKPGSDR TSQLVVRGRA VTTVGARDYI EHRGHLRTVV
AEELQSLRAD YDVVLCEGAG SPAEINLRAT DLANMGLARA ADLPVLVVGD IDRGGVLAHL
FGTVAVLAPE DQALIAGFVI NKFRGDVSLL APGLGQLTAM TGRPTLGVIP FAEDLWLDAE
DSLGVVGDAP VGRPAPPVGD DWLRVAAIRL PRISNSTDVE ALACEPGVSV RWVTDPSRLE
DADLVVLPGS KSTVSDLEWL RRNGIADAIA VHAKRGGPVL GVCGGYQMLG SVIVDDVESG
RGAVPGLGLL DLEVEFAPDK VLAQVRGDAH GVPVSGYEIH HGRVRRNGDP PLLHARGGAA
EGSIRGAVYG THWHGLLETD RFRRILLDDV AEHAGRTGFV TAPDTDVAAI RTAQLDLLAD
LVEQNLDLPA LQALLGAGAP AGLPVIASDL LR
