COBQ_NOSS1
ID COBQ_NOSS1 Reviewed; 493 AA.
AC Q8YUG9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=alr2377;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB74076.1; -; Genomic_DNA.
DR PIR; AB2103; AB2103.
DR AlphaFoldDB; Q8YUG9; -.
DR SMR; Q8YUG9; -.
DR STRING; 103690.17131469; -.
DR PRIDE; Q8YUG9; -.
DR EnsemblBacteria; BAB74076; BAB74076; BAB74076.
DR KEGG; ana:alr2377; -.
DR eggNOG; COG1492; Bacteria.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002483; 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..493
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141286"
FT DOMAIN 252..443
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 435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 493 AA; 54363 MW; AD1F044F52841AD5 CRC64;
MAMKSIMVVG TTSHAGKSLI STAICRILSR RGWRVAPFKG QNMALNAYVT ANGGEIGYAQ
AVQAWAAGVV PWVEMNPILL KPQGDMTSQV IIRGRPVGRV NAADYYEQYF EPGWRAIEES
LQHLATEFDL VVCEGAGSPA EINLKHRDLT NMRVAKYLNA PTLLVVDIDR GGAFAHVVGT
LELLDPEERQ LIKGVVINKF RGQRSLLDPG IKWLEERTGI PVVGVIPYLQ EVFPAEDSLD
LLERKTHKAH ADLQITVVRL PRIANFTDFD PLESEPTVAV KYISPKQDLG HPDAVILPGT
KTTIADLILL QKTGMAEAIQ NYAASGGTVL GICGGYQILG QMIADPEGIE GQAGRYQGLN
LLPIRTVITG QKIARQRQVS SNFPQQGLPV NGFEIHQGRS RVEPQGDSQA FQPLFDDVNL
GLVDSCQSVW GSYLHGLFDN GPWRRAWLNR LRQQRGLKSL PTGVANYREQ REQMLDNIAT
EVENHLDLTP FLP