ID   COBQ_PROM5              Reviewed;         510 AA.
AC   A2BXM3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=P9515_13271;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
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}.
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DR   EMBL; CP000552; ABM72534.1; -; Genomic_DNA.
DR   RefSeq; WP_011820631.1; NC_008817.1.
DR   AlphaFoldDB; A2BXM3; -.
DR   SMR; A2BXM3; -.
DR   STRING; 167542.P9515_13271; -.
DR   EnsemblBacteria; ABM72534; ABM72534; P9515_13271.
DR   KEGG; pmc:P9515_13271; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001589; 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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
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; PF01656; CbiA; 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..510
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002371"
FT   DOMAIN          262..460
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        452
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   510 AA;  57763 MW;  E85F0FB8BA3FA6D1 CRC64;
     MEFTENYNPK NKPIMVLGTS SGAGKSLTVT AICRILKKLG EEPIPFKGQN MSNNAWVDSN
     GGEMAYSQAL QAFSCGINPS SEMNPILLKP QGDSTSEVIH LGKSVGISTA KDYYKDWFMP
     GWEVIKKSIN IIYEKNKNCR LIIEGAGSPV EMNLIHRDLT NLRVAKYLDA SCILVTDIER
     GGVFAQIIGT LELMKPEERK LIKGILINRF RGDLSLFKEG KKWIEDKTKI PVLGIIPWLN
     DKFPPEDSLD LLERKSYLSN PEIKVGIIKL PSISNFSDFD PLENENSILI EWISEAQNLN
     QFDFIIIPGS KQTIKDQLFL NESGLSKEIK NYSHNNGNIF GICGGLQMLG TVLEDPFFKE
     GSNFNSDQSI KGIGLLPLKT TFLKHKITRQ IHSESIWPNS TKIIGFEIHN GITKLDSSHL
     DTLKTNHIFK DFDLGWYKEN REGGTIAGTY IHGIFENDEW RDHYINLIRK TKNKLTLDKK
     SRSYKMKRES IINNLANEFN NHFNISLLLN