COBQ_PELTS
ID COBQ_PELTS Reviewed; 525 AA.
AC A5D3N4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PTH_0958;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF59139.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D3N4; -.
DR STRING; 370438.PTH_0958; -.
DR EnsemblBacteria; BAF59139; BAF59139; PTH_0958.
DR KEGG; pth:PTH_0958; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006556; 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..525
FT /note="Cobyric acid synthase"
FT /id="PRO_1000074402"
FT DOMAIN 251..452
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 444
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 525 AA; 56170 MW; 64D2A7BA584E213A CRC64;
MAKAIMVQGT ASHVGKSILV TALCRIFRQD GYRVVPFKAQ NMALNSFVTA DGGEMGRAQV
LQAQAAGLEP AVEMNPVLLK PTGNAASQVI VLGKPVGNMS ARDYHLGKNQ DLLGIIEETL
RRLHREYEII VIEGAGSPAE VNLKERDLAN MRVSRLAGAP VLLVADIDRG GALAAVVGTL
ALLEPEEAEQ VRGIVINKFR GDRSLLDPAL EFLEARTGKP VLGVLPYLQG LRLPAEDSVC
LEEADTAAEG ELEIAVLYLP RISNFTDFDS LALEPGVRLR YVKDGEPLGS PDLVIIPGTK
NTTEDLLYLY ETGYAAAVRR AAAQGIPVCG ICGGYQMLGR ELRDVEHSES FRDELPGLGL
LDVVTTFVGE KILARARGEV CGGGPLFQEI AGLPVAGYEI HMGRTVLGEG TRPLLRVVER
EGGGGGDFDG AVAPSGLVWG TYFHGIFDND LLRAHLLGWL RRRRGLSQGT LEEKAGGGRG
STCLERELDR LAGAYRAHLN LEKIYALLGL PGPRLPRPGA GGGPK
