ID   COBQ_METPE              Reviewed;         487 AA.
AC   B8GDE3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mpal_1991;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
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; CP001338; ACL17294.1; -; Genomic_DNA.
DR   RefSeq; WP_012618613.1; NC_011832.1.
DR   AlphaFoldDB; B8GDE3; -.
DR   SMR; B8GDE3; -.
DR   STRING; 521011.Mpal_1991; -.
DR   EnsemblBacteria; ACL17294; ACL17294; Mpal_1991.
DR   GeneID; 7270797; -.
DR   KEGG; mpl:Mpal_1991; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002457; 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..487
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_1000116909"
FT   DOMAIN          246..431
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        325
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        423
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   487 AA;  52599 MW;  A804F068FE460549 CRC64;
     MSLMILGTSS HVGKSVTVAA ICRIMIRQGI SVAPFKSQNM SLNSYVTRDG AEIGIAQAMQ
     AFAARVLPSA LMNPVLLKPK GDSTSQVVLL GHPYKDVQIR DYYQETDHLL EIAVDAYHQL
     VEEYGAVIVE GAGGAAEVNL YDRDIANIRL AEHLRLPIVL VADIERGGVF AQVYGTIALL
     PEQIRPLVKG IIINKFRGDP TLFESGVKTL EDLTGVPVLG VIPYTRLDLP SEDSLSLQDK
     ERQTGLVRIA VIRLPQIANF TDFELLERHA AVDYLLPGES LDGYDCIIIP GTKNTVNDLL
     ALQASGTAAA IRDARGQGVP VIGICGGYQM LGKTVIDDGS EARKGTYEGL GLLDLVTTFE
     GYDKTTVQVQ RTAAPVPPIL DAMGTVSGYE IHMGTTVLKS GRTAFAGEGA VSDDGLVFGT
     YLHGLFMVPA AAEALLSYLY SQRGLTFTGI EEQNEDPYDL LADHFEAHLQ MERLLTLCSD
     HTPETPV