ID   COBQ_PARMW              Reviewed;         496 AA.
AC   Q7U5J9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; Synonyms=cobB;
GN   OrderedLocusNames=SYNW1704;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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; BX569693; CAE08219.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7U5J9; -.
DR   SMR; Q7U5J9; -.
DR   STRING; 84588.SYNW1704; -.
DR   EnsemblBacteria; CAE08219; CAE08219; SYNW1704.
DR   KEGG; syw:SYNW1704; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001422; 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..496
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141335"
FT   DOMAIN          255..445
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        336
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        437
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   496 AA;  54640 MW;  0E4FA8898D64930C CRC64;
     MNRKRPLMVL GTSSGAGKSL MTAALCRVLH RRGEQPLPFK GQNMSNNAWV DADGGEMAYS
     QAMQAWAAGL EPCCAMNPVL LKPRGDSTSE VIHGGTSVGL ARAEHYYRDW FRPGWQAIRE
     GLQTMQQRWP NGRLVLEGAG SPVEVNLQRR DLTNLRLAQY LRANCLLVAD IERGGVFAQI
     VGTLALLRPV ERPLIKGILI NRFRGRRELF DEGRSWLEQH TGVPVLGVMP WLNDLFPPED
     SLDLLERKPN RGPTDLEIAV LKLPSISNFS DLDPLEAEPS LRLRWVHPGD SLGSPDAVLL
     PGSKQTLRDL ETLRSSGLDR QLTAYATNGG SLLAICGGMQ LLGQELHDPE QLEGGDGAGP
     WPGLGLLPLT TEFGGTKALR QREVQALWPG TTPISGFELH HGSTWASDDL QPICNEPGLG
     WWCATPAGGC IAGTYLHGLL DNGPWRRRWL NQLRERKGLA PLITGLPHHG EHRHQLLERL
     ADAFEQHVDL TPLLQP