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Database: UniProt
Entry: COBQ_METMA
LinkDB: COBQ_METMA
Original site: COBQ_METMA 
ID   COBQ_METMA              Reviewed;         485 AA.
AC   Q8Q0P3;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=MM_0093;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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=AAM29789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM29789.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048045984.1; NC_003901.1.
DR   AlphaFoldDB; Q8Q0P3; -.
DR   SMR; Q8Q0P3; -.
DR   GeneID; 82159057; -.
DR   KEGG; mma:MM_0093; -.
DR   PATRIC; fig|192952.21.peg.106; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000595; 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; cd05389; CobQ_N; 1.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase.
FT   CHAIN           1..485
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_0000141350"
FT   DOMAIN          250..435
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   485 AA;  53324 MW;  329A8E85515528D0 CRC64;
     MEKKSLLILG TASHVGKSSV VTAICRILSR SYRVAPFKAQ NMSLNSWITK DGKEIGIAQA
     IQAKAAGTEP TADMNPVLLK PKGDCVSQVV LLGEPYADKS AGQYYDSIEE MHAVLKGALE
     RLWKEHDIIV MEGAGGAAEI NLYERDIVNV GTARLTKAPI ILVGDIERGG VFASLYGTIA
     LLPEDVRKNV KGFIINKFRG DIEILRPGLK QLEDKTGIPV LGVLPHFKLR IPSEDSVSLG
     DKEDSKAEKE IEVAVIRLPR ISNFTDFEPL EGLVKVRYVD INEELGNPDA IMIPGTKNTV
     NDLLDLRASG MDKKIQAFKG KVPIFGICGG YQMLGRTIFD SGVENGVEAE FEGLGLLDIG
     TRFGEYKKRT VQVTKKVNGY GPILRPIDGE EIKGYEIHMG VTDSNRTVFG DDGAIDEDGF
     VIGTYLHGLF DNRNIRNALV RYLYEKKGLE YEPDEAISEN DAYEELANVV EQNIDMEKLF
     EIAGV
//
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