COBQ_BACFR
ID COBQ_BACFR Reviewed; 495 AA.
AC Q64TD9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BF2491;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD49240.1; -; Genomic_DNA.
DR RefSeq; WP_005787973.1; NZ_UYXF01000003.1.
DR RefSeq; YP_099774.1; NC_006347.1.
DR AlphaFoldDB; Q64TD9; -.
DR SMR; Q64TD9; -.
DR STRING; 295405.BF2491; -.
DR EnsemblBacteria; BAD49240; BAD49240; BF2491.
DR KEGG; bfr:BF2491; -.
DR PATRIC; fig|295405.11.peg.2399; -.
DR HOGENOM; CLU_019250_2_2_10; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002197; 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_0000141287"
FT DOMAIN 256..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 55071 MW; A13CC2733DE7082C CRC64;
MNKNLHPLML AGTGSDVGKS IIAAAFCRIF LQDGYHPAPF KAQNMALNSY ATPEGLEIGR
AQAVQAEAAG VPCHTDMNPL LLKPSSDHTS QVVLNGRPIG NRNAYEYFRR EGREELRKEV
HAAFDRLAAR YNPVVMEGAG SISEINLRDS DLVNLPMAMH AGADVILVAD IDRGGVFASV
YGSVMLLRPE ERKHIKGILI NKFRGDIRLF ESGVKMLEDL CGVPVVGVVP YYKDIYIEEE
DSVMLQTKNI RAGQGKVNVA VVLLRHLSNF TDFNVLERDP RVHLFYTNNT DELMKADIIL
LPGSKSTLSD LYELRRNGVA QAIVRAHREG ATVMGICGGY QLMGREVCDP DHVEGEIERL
PGLGLLPVST RMQGEKVTRQ VRFRFLEDSA VCEGYEIHMG TTTPLADVPV SPLNHLADGR
EDGYFVDRTC MGTYVHGILD NPSVIDYLLE PFADKLKETA FDYKAFKEEQ YDKLAAHVRK
HVDLPLIYQI LTDND
