ID   COBQ_PROMA              Reviewed;         507 AA.
AC   Q7VB41;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, 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}; OrderedLocusNames=Pro_1259;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00303.1; -; Genomic_DNA.
DR   RefSeq; NP_875650.1; NC_005042.1.
DR   RefSeq; WP_011125410.1; NC_005042.1.
DR   AlphaFoldDB; Q7VB41; -.
DR   STRING; 167539.Pro_1259; -.
DR   EnsemblBacteria; AAQ00303; AAQ00303; Pro_1259.
DR   GeneID; 54200593; -.
DR   KEGG; pma:Pro_1259; -.
DR   PATRIC; fig|167539.5.peg.1321; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_3; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001420; 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; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141317"
FT   DOMAIN          259..456
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        340
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        448
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   507 AA;  56154 MW;  F7B8F7379D2F5E75 CRC64;
     MKNISAGHNA LMVLGTSSGA GKSIITTAIC RSLLRKGEVP IPFKGQNMSN NAWVDINNGE
     MAYSQAVQAW AAGIEPICAM NPVLLKPQGD CTSEVIHLGK SVGVVQAANY YEDWFSSGWE
     AIQKGLNDIA TSYKKHRLIL EGAGSPVEIN LQHRDLTNLK LAKHLNAKCV LVADIERGGV
     FAQIIGTLAL LKPDEKALIQ GIIINRFRGD ISLFEKGRQW IEEESKIPVL GIMPWLNEIF
     PPEDSLDLLE RKHKKTKAEI QIAVIKLPSL SNFADLDPLE AEPTIQLNWI QPGDYLGNPN
     AVIIPGSKQT LKDLQSLQSS GLGNQIKEFA SSGGTVFGIC GGLQILGEKL EDPLGIEQSF
     LETSISELEG LSLIPIKTIF HSKKSLTKKD VISKWPDESR IMGFELHHGE STPTNSQKVK
     VKDLCNETSL GWVNEECNPI KAAGTYLHGI FDNGTWRRLW INQIRKKANL YELPLLEENH
     DAKREKVINR LTDVFEENIN LEYLLKT