ID   COBQ_PARD8              Reviewed;         496 AA.
AC   A6LBQ5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BDI_1360;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(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; CP000140; ABR43119.1; -; Genomic_DNA.
DR   RefSeq; WP_005856411.1; NC_009615.1.
DR   AlphaFoldDB; A6LBQ5; -.
DR   SMR; A6LBQ5; -.
DR   STRING; 435591.BDI_1360; -.
DR   EnsemblBacteria; ABR43119; ABR43119; BDI_1360.
DR   KEGG; pdi:BDI_1360; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_10; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   BioCyc; PDIS435591:G1G5A-1399-MON; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000566; 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; Reference proteome.
FT   CHAIN           1..496
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002369"
FT   DOMAIN          257..447
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        338
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        439
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   496 AA;  55029 MW;  D249768389C618CC CRC64;
     MKQHLRPIMF VGTCSDAGKS VINAAFCRIF KQDGYQPAPF KAQNMSLNSY STPEGGEMGR
     AQVVQAEACG ISPHTDMNPI LLKPTNDKSS QVVLNGKPVG NMSAKDYFGI QNQKEELFKE
     AIEAFKRLEA RYNPIVLEGA GSISELNLRD RDITNMRMAI AAGASTYLVA DIDRGGVFGS
     VYGTIALLRP EERVLMKGVI INKFRGDASL FEEGRSLLKE LTGIPVVGVI PWFRDIKIEE
     EDSVALDMKN NTYKDGKINV AIILLKRMSN FTDFDVLEMD PRFNPYYTNN IDEIEKADII
     LLPGSKNTLS DLQSLRANGI AMAIIRAHKA GKKVIGICGG YQMMGVRLED PESIEGNIPA
     IPGLGLLPQC TVIEQEKITR QSDFAFLPSS ENKDCKGYEI HMGRTTLLGD APEQPVARLE
     DGRTDGYYLN NRCWGSYMHG ILDNPAVLDN LAEGFDTETT TGPFDYAAFK EEQYDKLAAL
     VREHVDMEYI YNSIKN