COBQ_METNO
ID COBQ_METNO Reviewed; 489 AA.
AC B8IUQ6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mnod_2141;
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) 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; CP001349; ACL57124.1; -; Genomic_DNA.
DR AlphaFoldDB; B8IUQ6; -.
DR SMR; B8IUQ6; -.
DR STRING; 460265.Mnod_2141; -.
DR EnsemblBacteria; ACL57124; ACL57124; Mnod_2141.
DR KEGG; mno:Mnod_2141; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; DVRMNPL; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008207; 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..489
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116908"
FT DOMAIN 254..442
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 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 489 AA; 51414 MW; A87C289B63A24607 CRC64;
MTARTLMIQG TGSDVGKSLI VAGLSRAFAR RGLRVRPFKP QNMSNNAAVT AEGGEIGRAQ
ALQARAACVA PSVHMNPVLL KPQSETGSQV VVQGRRVGTA KAREYQAWKP RLLSAVLDSF
DHLRAEADLV LVEGAGSASE VNLRAGDIAN MGFARASGTP VVLLGDIDRG GVIASLVGTK
AVLDPDDAAM IRGFLVNRFR GDPSLFADGM ALIAARTGWA ALGLIPHFPE AARLPAEDVL
GLKGSVRPSA RPGARVIAVP VLPRIANFDD LDPLRAEPGV SVVLVEPGRP LPAEADLVLL
PGSKTTIADL IAFRAEGWDI DLAAHVRRGG RVLGLCGGYQ MLGRRIEDPH GIEGEVRAVD
GLGLLDVVTV MTPDKRLAAV TGASLPDETP FCGYEMHLGE TRGPDAARPL LRFADGRPDG
AVSADGRVCG TYVHGLFADD RQRALWLERL GTSSAGEAYE AGIDAVLDRL AEHLERHVAC
DALLALAAG