ID   COBQ_PROM9              Reviewed;         509 AA.
AC   Q319X7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN   OrderedLocusNames=PMT9312_1259;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) 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; CP000111; ABB50318.1; -; Genomic_DNA.
DR   RefSeq; WP_011376805.1; NC_007577.1.
DR   AlphaFoldDB; Q319X7; -.
DR   SMR; Q319X7; -.
DR   STRING; 74546.PMT9312_1259; -.
DR   EnsemblBacteria; ABB50318; ABB50318; PMT9312_1259.
DR   KEGG; pmi:PMT9312_1259; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002715; 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.
FT   CHAIN           1..509
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002372"
FT   DOMAIN          262..459
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        343
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        451
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   509 AA;  57798 MW;  75BB5C76B5D20FC7 CRC64;
     MYLEEKLHKI KKPIMVLGTS SGAGKSLTVT AICRILKNLA EQPIPFKGQN MSNNAWVDWE
     GGEMAYSQAL QAFACGVNPS SEMNPILLKP QGNSVSEVIH LGKSIGTTSA KNYYQDWFIP
     GWEVIKKSLN SIYKKNPNCR LIIEGAGSPV EMNLKHRDLT NLKIAKYLKA NCILVTDIER
     GGVFAQIIGT LELMKPEEKK LIKGIIINRF RGDLSLFEEG KKWIEEKTQI PVIGIVPWLN
     DSFPPEDSLD LLENKSRFTN AEIKVGIIKL PSISNFSDFD PLENEESILI EWIRESQNLK
     KYDFIILPGS KQTIKDQMFL EKTGLSHDLR EYSNNKGHII GICGGLQMLG TFLEDPFLKE
     GSKTFSEQKI KGIGLLPLRT TFFEEKLTRQ ISSESLWPCQ SKINGFEIHN GQTELDNTQN
     SLKINPIFKD LNLGWYKENK EGGTIAGTYI HGIFENDIWR DQYINLIRMN KKLPALKKRT
     SSYKNKREKI IENLANEFNK HLNLSSLLN