COBQ_THEPX
ID COBQ_THEPX Reviewed; 507 AA.
AC B0K2J6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Teth514_0300;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
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., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) 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; CP000923; ABY91616.1; -; Genomic_DNA.
DR RefSeq; WP_009051853.1; NC_010320.1.
DR AlphaFoldDB; B0K2J6; -.
DR SMR; B0K2J6; -.
DR EnsemblBacteria; ABY91616; ABY91616; Teth514_0300.
DR KEGG; tex:Teth514_0300; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002155; 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.
FT CHAIN 1..507
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116437"
FT DOMAIN 249..451
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 443
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 507 AA; 56874 MW; 05D5444E77E0F4B6 CRC64;
MALKLMIQGT ASSVGKSLLV AAFCRIFKQD GYRVAPFKSQ NMALNSYITD EGLEIGRAQA
MQAEAAGVKP SYHMNPILLK PSSDKKSQVV LRGKVYKNMS AAEYHQFKPQ LLKFIKEDFD
FLASQNDIVV IEGAGSPAEI NLRDRDVVNM GMAEMVNAPV LLVGDIDKGG VFASIAGTLL
LLKENERNRI EGVLINKFRG DIEILKPGLE MLENIVHKKV LGVVPYMDVH IDEEDGATER
FYRRSTEGDI EIAVINLPHI SNFTDFEPLA KVPGVKLRYV NKGERIGDCD VVIIPGTKNT
IGDLQALKGY RLDKEIFEMR KKGKFIVGIC GGYQILGKVI KDPGRIESTT SEIEGLGLLD
VETVIENEKT TTQIKAVIRN NLPSILSPLR NIAVEGYEIH MGKSRILGDC QPFSVITHRN
GEKIEVYDGC ISDDGKVFGT YIHGIFENRE FVREFINIVR KSKGLSPIEE IIDYKEFKER
EYDKLADIVR KSIDMKKVYE IMERYKD