ID   COBQ_SPHAL              Reviewed;         485 AA.
AC   Q1GPG1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Sala_2756;
OS   Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS   (Sphingomonas alaskensis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=317655;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000356; ABF54461.1; -; Genomic_DNA.
DR   RefSeq; WP_011543026.1; NC_008048.1.
DR   AlphaFoldDB; Q1GPG1; -.
DR   SMR; Q1GPG1; -.
DR   STRING; 317655.Sala_2756; -.
DR   EnsemblBacteria; ABF54461; ABF54461; Sala_2756.
DR   KEGG; sal:Sala_2756; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000006578; 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; Reference proteome.
FT   CHAIN           1..485
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332390"
FT   DOMAIN          250..436
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   485 AA;  50449 MW;  2FD8AEDAC17EB211 CRC64;
     MAALMLQGTG SDVGKSVLVA GLCRALANRG LRVRPFKPQN MSNNAAVTID GGEIGRAQAL
     QALACRTPPH SDMNPVLLKP QADRTSQLIV HGRVRGTLGS GNFRAGRGAL LPDVLESYGR
     LRRQCDIVIV EGAGSPAEIN LRAGDIANMG FARAARVPVV LVGDIDRGGV IAAIVGTRTV
     IDAEDAAMIK GFVINKFRGD PALFDDGYRA IAERSGWPGL GVVPWLAAAA RLPSEDAVIL
     ERRADAREGR RIVACPILPR IANFDDLDPL KQEPGVELLM VPPGQPIPAE AAIIVLPGSK
     ATIADLAALR REGWDIDIKA HHRRGGLILG LCGGYQMLGT RIADPLGIEG AASEVEGLGL
     LDVTTELAPA KTLREVTGTA WNSPVAGYEM HMGATVGTDT ARPFARIDGG GGEGAINAAG
     NVIGTYIHGL LASPALRSAL LAKIGVAGNG RDHGADVDAA LDDIAAELAI HIDIGALLRI
     AAHPV