COBQ_THEGJ
ID COBQ_THEGJ Reviewed; 483 AA.
AC C5A475;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=TGAM_0535;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS33037.1; -; Genomic_DNA.
DR RefSeq; WP_015858155.1; NC_012804.1.
DR AlphaFoldDB; C5A475; -.
DR SMR; C5A475; -.
DR STRING; 593117.TGAM_0535; -.
DR PaxDb; C5A475; -.
DR EnsemblBacteria; ACS33037; ACS33037; TGAM_0535.
DR GeneID; 7987403; -.
DR KEGG; tga:TGAM_0535; -.
DR PATRIC; fig|593117.10.peg.531; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001488; 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..483
FT /note="Probable cobyric acid synthase"
FT /id="PRO_1000201972"
FT DOMAIN 247..433
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 425
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 483 AA; 54069 MW; F4B1E31E81A19F7E CRC64;
MGKALMVLGT SSGAGKSLLV TALCRIFSNL GYDVVPFKSQ NMSLNSAPSI EGGEISRAQY
LQAIACRKKP SVRFNPILLK PEGNMRSQVI FMGKPIGSVS AKDYMLSRKE ELFRKAMKVL
DELKERHDLV IIEGAGSPVE INLKDYDIAN TRVMLHAKAK GILVTDIDRG GSFASIVGTM
ELLKPEERDT IIGFVFNKFR GDKSLLEPGF EYLEKRYGKP TLGVIPYVEH RLPEEDSLAE
FPKVKGELHI QIIKLPHISN FTDFEPLHWA NGVDYVTRPE ELKGDVIIIP GSKNTVEDLL
WLRENGFEDA IIEAHREGSF VVGICGGFQM LGEKIIDTVE SKRGEVKGIG LLPAKTVFEK
TKRTNHLNAE VLWEPARGMA VEGYEIRFGR SVSERPFSVI KAINGAKTFE PEGAIGERAF
GTYLHGIFHN FAFTERFLNF LRVEKGLEPV SIERWSIEEE IERFAKLVEE NIDVERILGE
LGL