ID   COBQ_PROA2              Reviewed;         493 AA.
AC   B4S8A8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Paes_1269;
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001108; ACF46295.1; -; Genomic_DNA.
DR   RefSeq; WP_012505830.1; NC_011059.1.
DR   AlphaFoldDB; B4S8A8; -.
DR   SMR; B4S8A8; -.
DR   STRING; 290512.Paes_1269; -.
DR   EnsemblBacteria; ACF46295; ACF46295; Paes_1269.
DR   KEGG; paa:Paes_1269; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_10; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002725; 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..493
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000090239"
FT   DOMAIN          253..446
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   493 AA;  53751 MW;  A46656F53123E3B7 CRC64;
     MKNLAVFGTA SDVGKSVIAT ALCRIFSNEG IDVAPFKAQN MSNNSGVTPD GFEIGRAQVV
     QAEAARVVPT ADMNPVLLKP NTDTGAQVVL QGKAVANRSA RDYFGNTRPW AEAAFESLRR
     LQAAHDMLVI EGAGSCAEMN LYDRDFVNFK TAEAADAPVI LVADIDRGGV FAQVIGTVSV
     LPPEAKARIS GVLVNRFRGD ISLFEDGVRF LEEHSGIPVL GVVPFFRGFS IDSEDAVPLQ
     TIVDPSGSPD PGKISIAVIY FPHISNFTDF AVLEREEGVE LHYLHHAKAL DGYQAVILPG
     SKNVRGDIEW LRQQGWESRL EDFRRNGGVI AGICGGYQML GRSIADPYGV EGVPGRTAGL
     DLLPVETVLQ QEKTLCNARG VMSGNGYSVH GYEIHMGETS CHGDALPLFD VTTRNGIAVS
     ARDGVMTSDT KVFGTYFHGV FDAPLFRHWF FRQLSASYTP SERTEDRDED YNRLARHVAA
     HLDLDKLYRI IEK