COBQ_SYNJB
ID COBQ_SYNJB Reviewed; 499 AA.
AC Q2JJP4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CYB_2173;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
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; CP000240; ABD03118.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2JJP4; -.
DR SMR; Q2JJP4; -.
DR STRING; 321332.CYB_2173; -.
DR KEGG; cyb:CYB_2173; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001938; 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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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..499
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332393"
FT DOMAIN 266..449
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 441
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 499 AA; 55355 MW; 6981A8C3737348ED CRC64;
MSCSGRSLMV VGTSSHVGKT LLVTALCRIL KKAGKRVAPF KAQNMSLNAY VTPDGKEIAY
AQALQAWAAG IPPAVEMNPI LLKPQGNLTS QIVLNGVAVG TYRAGEYYER WFAPAWQAVK
EALARLQKQY DWILCEGAGS PAEVNLKHRD LANMRVALHL GSPTWLVADI DRGGALAHVV
GTLQLLEPEE RALIRGIVIN KFRGSRELLQ PGLDWLENYT GIPVVGVLPW VDWVLPQEDS
MGIAANPLLW EDRRDRAGGQ ALREGRLEIA VVRLPQVANF SDFDPLLAEP TVHLRWVHPG
QSLGSPDVVI LPGSKTTLND LFALQKTGLA EQLRQYSGHI VGICGGLQML GETIADPEGW
EGIAGTYSGL GFLPLTTVLQ PTKVTQQVQT QSRWPALAPI QGYEIHQGST QADPSGCLPL
FDRENLGWRD PTGRIWGSYL HGLFDNHLWR RQWLNWLRRQ KGWDPLPELE GHYAQQREQL
LERLADLWQP HLDLGLLME
