ID   COBQ_SHEAM              Reviewed;         496 AA.
AC   A1S3L6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Sama_0765;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABL98972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000507; ABL98972.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A1S3L6; -.
DR   SMR; A1S3L6; -.
DR   STRING; 326297.Sama_0765; -.
DR   PRIDE; A1S3L6; -.
DR   EnsemblBacteria; ABL98972; ABL98972; Sama_0765.
DR   KEGG; saz:Sama_0765; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000009175; 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..496
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332386"
FT   DOMAIN          251..449
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        441
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   496 AA;  53039 MW;  4C610153B56ECFB1 CRC64;
     MIQGTASDAG KTTLVAGLCR LLARQGLKVA PFKPQNMALN SAVTEDGGEI GRAQALQAAA
     CGLKPHTDFN PILLKPGSDT RAQVIVHGKA LTSLEASAFF GPEGKGYKAI AIEAVLESYN
     RLKQSFDYLL VEGAGSPAEI NLRENDIANM GFAEAVDCPV ILVADIDKGG VFAQLVGTLA
     LLSESEQARI KGFVINRFRG DINLLQPGLD WLEAHTGKPV LGVVPYLHNL LLDAEDALVP
     YQQAGADSGA RFRVRVLVYP RTSNHTDFDP LRLHPGVDFD YLDIQHASPD ALQGADLVIL
     PGSKNVRADL ECLKTKGFDC ALRKHVRYGG KLVGICGGYQ MLGIEIDDPD GVEDTPGSSD
     ALEFLPLITE LEGSKVLANV SGELSLGEEA VAVKGYEIHC GRTTVLGQLS RPLFLVDDTG
     NPASDRGCIS DDGAIFGCYL HGIFDTPAAL DAVLAWAGYR GAARGTSLEE HREQQLERLA
     DTLAEHLDMA RLNSLF