COBQ_SYNP6
ID COBQ_SYNP6 Reviewed; 491 AA.
AC Q5N2H9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=syc1301_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008231; BAD79491.1; -; Genomic_DNA.
DR RefSeq; WP_011243613.1; NC_006576.1.
DR AlphaFoldDB; Q5N2H9; -.
DR SMR; Q5N2H9; -.
DR STRING; 269084.syc1301_c; -.
DR EnsemblBacteria; BAD79491; BAD79491; syc1301_c.
DR KEGG; syc:syc1301_c; -.
DR eggNOG; COG1492; Bacteria.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001175; 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..491
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141334"
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; 54579 MW; B747CCC2E60F3ADE 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 IDALSDAVEP
YLNLSPLLTA L
