COBQ_META3
ID COBQ_META3 Reviewed; 493 AA.
AC A6UWF6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Maeo_1252;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000743; ABR56828.1; -; Genomic_DNA.
DR RefSeq; WP_011973960.1; NC_009635.1.
DR AlphaFoldDB; A6UWF6; -.
DR SMR; A6UWF6; -.
DR STRING; 419665.Maeo_1252; -.
DR EnsemblBacteria; ABR56828; ABR56828; Maeo_1252.
DR GeneID; 5327060; -.
DR KEGG; mae:Maeo_1252; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001106; 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..493
FT /note="Probable cobyric acid synthase"
FT /id="PRO_1000002363"
FT DOMAIN 252..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 493 AA; 55191 MW; 36E95DCEAFE99ADE CRC64;
MAKFIMVVGT SSNSGKTVLV AGICRILANK GYKVAPFKSQ NMSLNSRVAN EDGEIAVAQY
TQSLASKVEP SIHFNPILLK PMGNFVSQVI VQGAPYKTIN YNEYREDKEY YLTKIKESLE
YLNKNYDFVV MEGAGSCCEI NLLGDDIANL RIAELSNADA ILVSDIDRGG VFASLYGTVE
LLPQKWKKLI KGFVINKFRG NAEVLIDGYK KIEELTNIPV LGTIPYSEEL ELPEEDSQAL
QNKKVFGNIN SPVEVNVVRF SKISNFTDID AFSKDALIKF IDFKEDITGD ILILPGTRCS
TVEMDLMKKY KMDKKIKDFA KKGGIVIGIC GGYQTMGKML IDDTHSEGDI GTIEGIGLFD
METYFGNKKA IVNSNGILSI KDDDFLVNGY ELHEGITHSN EKPLIKLNKG FGNKNDGYDG
SINIKDGNYL IGTYFHGIFD NYEFRNHIIN MVLAEKGHKL ITEDNYKDNF EKNINKFAEI
IENNVNLEKI FKK