COBQ_SYNJA
ID COBQ_SYNJA Reviewed; 495 AA.
AC Q2JRG5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CYA_2678;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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}.
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DR EMBL; CP000239; ABD00789.1; -; Genomic_DNA.
DR RefSeq; WP_011431460.1; NC_007775.1.
DR AlphaFoldDB; Q2JRG5; -.
DR SMR; Q2JRG5; -.
DR STRING; 321327.CYA_2678; -.
DR PRIDE; Q2JRG5; -.
DR EnsemblBacteria; ABD00789; ABD00789; CYA_2678.
DR KEGG; cya:CYA_2678; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008818; 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..495
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332394"
FT DOMAIN 262..445
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 340
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 437
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 54547 MW; 250C5C2E27A8872C CRC64;
MSSACRSLMV VGTSSHVGKT LLVAALCRLL KKAGKKVAPF KAQNMSLNAY VTPEGHEIAY
AQALQAWAAG IPPAVEMNPI LLKPQGNLTS QVVLNGVAVD TCRAGEYYER WFAPAWEAVK
TALARLQQQY EWIICEGAGS PAEVNLKHRD LANTRVALHL GSPTWLVADI DRGGALAHVV
GTLQLLEPAE RALIRGIVIN KFRGARELLQ PGLDWLENYT GIPVVGVLPW LDWVLPQEDS
MGLEAGPQLW ENRRERAGRG SCLEIAVIRL PQVANFSDFD PLLAEPSVHL RWVHPGQSLG
SPDVVILPGS KTTLKDLLAL QKTGLADQLR LYSGHIVGIC GGLQMLGQTI ADPAGLEGVA
GTYPGLGFLP LTTVLQPTKV TQQVQTQSRW PAPAPVQGYE IHQGSTQADP AGCLPIFEQE
GLGWRDPTGR VWGSYLHGLF DNHRWRRHWL NELRRQKGWD PLPELEGHYA QQREELLDCL
AEAWRPHLEW QQLLE
