ID   COBQ_RIPO1              Reviewed;         495 AA.
AC   B7JVZ0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN   OrderedLocusNames=PCC8801_1628;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001287; ACK65679.1; -; Genomic_DNA.
DR   RefSeq; WP_012594952.1; NC_011726.1.
DR   AlphaFoldDB; B7JVZ0; -.
DR   SMR; B7JVZ0; -.
DR   STRING; 41431.PCC8801_1628; -.
DR   EnsemblBacteria; ACK65679; ACK65679; PCC8801_1628.
DR   KEGG; cyp:PCC8801_1628; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008204; 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..495
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000116434"
FT   DOMAIN          250..444
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        331
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;  54664 MW;  6593394FCDB62E46 CRC64;
     MKAIMVVGTT SHAGKSFITT AICRILARQG WHVTPFKGQN MALNAYVTPT GGEIGHAQAV
     QAWAAKITPS VDMNPILLKP QGNMTSQVII HGQAVGTTSA QEYYEQYFDR GWKAITSSLD
     CLASEYDVVV CEGAGSPAEI NLKHRDLTNM RVAHHLNAAT ILVVDIDRGG AFAHVVGTLQ
     LLEPEEKALI KGIVINKFRG QRSLLDSGIE WLENYTSIPV LGVIPWREIM FPSEDSLGLL
     DRPSYRSTTS LKISILRLPH ISNFTDFDPL DAETTVNLNY LDLRGTLGYP DAVIIPGSKT
     TIADLIALHT TGMAQQLQDY VSAGGVILGI CGGFQMLGQT VFDPDQLEGG QKAYKGLNLL
     PLETIITSNK IVRQRQIMSN YPYSGLPVTG YEIHQGITQL IQSYETEQTI LLDQLFDDIS
     LGFVNESQTI WGCYLHGLFD NGAWRRSWLN YLRQRRGLPS LPTGIANYRE QREANLDAIA
     DLVEEFVNLK PVFPK