ID   COBQ_PROM2              Reviewed;         509 AA.
AC   A8G5V0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=P9215_13661;
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV50981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000825; ABV50981.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041484398.1; NC_009840.1.
DR   AlphaFoldDB; A8G5V0; -.
DR   SMR; A8G5V0; -.
DR   STRING; 93060.P9215_13661; -.
DR   EnsemblBacteria; ABV50981; ABV50981; P9215_13661.
DR   KEGG; pmh:P9215_13661; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002014; 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_0000332362"
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;  57493 MW;  F4790B13B5B60258 CRC64;
     MDLEAKLHEI RKPIMVLGTS SGAGKSLTVT AICRILKNLG EEPIPFKGQN MSNNAWIDWE
     GGEMAYSQAL QAFACGINPS AEMNPILLKP QGNSTSEVIH LGKSIGTTTA QNYYKDWFIP
     GWEVIKKSLK SIYELNPNCR LIIEGAGSPV EMNLIHRDLT NLRVAKYLNA NCLLVTDIER
     GGVFAQIIGT LELMKPEERK LIKGIIINRF RGDLSLFEDG KKWIENKTQI PVIGIIPWLN
     DSFPPEDSLD LIEKKSLSKN HEIKVGIIKL PSISNFSDFD PLENEETILI EWIRKSKNLS
     TYDFIILPGS KQTIKDQKFL ENSGLSQDIR DYSNNEGNII GICGGLQMLG TTLEDPYFKE
     GAKNYSEQKI NGIGLLPLKT TFFKKKLTRQ INTKSIWPCQ SQINGFEIHN GQTILDDSQS
     SLKINPIFED LDLGWFKENN KGGTIAGTYI HGIFENDSWR EQYINLIRKS KNLPILNKKS
     ISYKKKRESI IDNLANEFHK HLNLTSFLS