COBQ_PICTO
ID COBQ_PICTO Reviewed; 469 AA.
AC Q6L0V5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PTO0812;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43397.1; -; Genomic_DNA.
DR RefSeq; WP_011177613.1; NC_005877.1.
DR AlphaFoldDB; Q6L0V5; -.
DR SMR; Q6L0V5; -.
DR STRING; 263820.PTO0812; -.
DR EnsemblBacteria; AAT43397; AAT43397; PTO0812.
DR GeneID; 2844066; -.
DR KEGG; pto:PTO0812; -.
DR PATRIC; fig|263820.9.peg.848; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000438; 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..469
FT /note="Probable cobyric acid synthase"
FT /id="PRO_0000141354"
FT DOMAIN 241..427
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 419
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 469 AA; 51658 MW; 3FBB676D36DC6F9C CRC64;
MKMIQVLGTS SDSGKSTLAT AFCRILKDLG YRVSPFKAVN MSLNSIAIKD GSEIARAQWV
QAMAAGAEPS AYMNPVLLKP EGHHKSQVII LGRSIGSMGI NDYYNYINKN AKIIKESIDF
LSNKYDVIIS EGAGSPAEIN LAGRDFANIY VSSLYNTPAI LVADIDRGGV FASIYGTINL
MQRSDLLKYY IINKMRGDQS LLYPGIERIE ELTGKKCLGI VPYIDLKLPG EDSLDYNFSG
SGSIGIVRYP YMENYSDFDP LIFNEKAFYI KNKEDLKRCD VIILPGSKDV FHDLEYINSN
GIADSIKRCS GEKMIIGICG GYQMLGKRIN DASGVESDGV SIPGLGLLDI ETYYNKTKTT
GSVKYRFAEN QLKINGSGTG YEIHYGSIVK NNEMPLLITD HGPEGSVSSN GMVIGTNVHG
ILENNEFYRY ITGEYLDYDN IIENSIETLA GIVKKSINIE GFLELLNDA