ID   COBQ_GLOVI              Reviewed;         490 AA.
AC   Q7NJR0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=glr1772;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC89713.1; -; Genomic_DNA.
DR   RefSeq; NP_924718.1; NC_005125.1.
DR   RefSeq; WP_011141770.1; NC_005125.1.
DR   AlphaFoldDB; Q7NJR0; -.
DR   SMR; Q7NJR0; -.
DR   STRING; 251221.35212338; -.
DR   EnsemblBacteria; BAC89713; BAC89713; BAC89713.
DR   KEGG; gvi:glr1772; -.
DR   PATRIC; fig|251221.4.peg.1804; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   InParanoid; Q7NJR0; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   PhylomeDB; Q7NJR0; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000557; 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..490
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141304"
FT   DOMAIN          250..432
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        424
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   490 AA;  53242 MW;  08B9F9946DFFF231 CRC64;
     MAALMVVGTS SHAGKSLLVT ALGRLFHRRG VKVAPFKGQN MALNAYVTAE GHEIGHAQAV
     QAWACGLEPS VAMNPILLKP QGNMTSQVIL KGKPAGVCGA VDYYRDYFEP GWQAVVEALA
     ELQSQYELVI CEGAGSPAEV NLRHRDLTNM RVALHLGAPT LLVTDIDRGG ALAHVVGTLQ
     VLPPEERALI KGIVINKFRG SLALLQPGLD WLAQYTGVPV VGVLPWLEMA LPEEDSMGLF
     DRRGARKQAQ LEIVVIRLPR IANFTDFDAL EAEPSVRVRY VSPDGYLGHP DAIILPGSKA
     TIPDLLALEA SGMAAQIRAY GGVILGICGG LQILGSTIDD PEGFEGHPGR HPGLGLIEAT
     TVFEPLKITR QVQVESRLPA GEPVVGYEIH QGQTTFAPTL EALFAEPHLG VVSSNRRVWG
     TYLHGLLDNH AWRRHWLNAL RERRGLPQLP VQSGHYREQR EEMFERLADA WEPHLPIDGF
     AQLAGFASQV