COBQ_SYNE7
ID COBQ_SYNE7 Reviewed; 491 AA.
AC Q31RS6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, 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};
GN OrderedLocusNames=Synpcc7942_0211;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; CP000100; ABB56243.1; -; Genomic_DNA.
DR RefSeq; WP_011377496.1; NC_007604.1.
DR AlphaFoldDB; Q31RS6; -.
DR SMR; Q31RS6; -.
DR STRING; 1140.Synpcc7942_0211; -.
DR PRIDE; Q31RS6; -.
DR EnsemblBacteria; ABB56243; ABB56243; Synpcc7942_0211.
DR KEGG; syf:Synpcc7942_0211; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0211-MON; -.
DR UniPathway; UPA00148; -.
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..491
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332395"
FT DOMAIN 250..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 491 AA; 54563 MW; A9462CC2E60F3ADE CRC64;
MPALMVVGCT SHAGKSLITA AICRLLRRQG WRVAPFKGQN MALNAYVTAS GGEIGYAQAF
QAWAAGVEPT IEMNPILLKP QGDMTSQVVL KGRAVGRTLA ERYYQDYFEV GWEAICEALE
QLQADYDWIV CEGAGSPAEI NLKHRDLTNL RVAKHLQAPT LLLVDIDRGG SFAHLIGTLE
LLDPDERSLI RGFVFNKFRG RRELLQSGLD WLEERTGIPV LGVIPWIDRA FPSEDSLDLM
ERRRRKTQAE VTIAVIRLPR IANFTDFDPL ESEPSVQVRY VGLQDELGYP DAVILPGSKT
TISDLLDLQR SGLAQAIRDY AAAGGTVLGI CGGFQMMGQH ILDLEGTEGI EGQFEGLHLF
PTQTWFTAEK TLRQRQTTAR SPQAGLPITG YEIHQGQTRL DSDSEEFLPI FDDPKLGLCD
RNGNLWGTYL HGIFDNGAWR RAWLNSLRHR RGLKALPTSI GHYQAQRDDL IDALADAVEP
YLNLSPLLTA L
