COBQ_METKA
ID COBQ_METKA Reviewed; 494 AA.
AC Q8TVH5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=MK1414;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02627.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TVH5; -.
DR SMR; Q8TVH5; -.
DR STRING; 190192.MK1414; -.
DR EnsemblBacteria; AAM02627; AAM02627; MK1414.
DR KEGG; mka:MK1414; -.
DR PATRIC; fig|190192.8.peg.1570; -.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001826; 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..494
FT /note="Probable cobyric acid synthase"
FT /id="PRO_0000141349"
FT DOMAIN 249..447
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 439
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 494 AA; 54561 MW; 90CE8D5F1C8D84E0 CRC64;
MSAIMFVGTA SNSGKSFLAA VTCAYLRQRG VDVAPFKSQN MSLNSCVAKE NGEIAVAQAF
QAAMAGQEPS IHHNPVLLKP KGELRSEVIV HGKPIGTMSY REYREIVFED PWQAVLESAE
ILSEEHEVIV AEGAGSPAEI NVLDTDIANL RVAEALGADV ILVADISRGG AFAAVYGTIE
LLPERWRRLI KGFLFNKFLG DESLLEPGIK ELERRLGVRY LGTVRHVGDF WMPWEDSEAL
DTHSPGRGSV RIAVIRLPRI SNFTDFEPLA MEPDVRVEFV DPRDNLPEDA DAVILPGTRT
TISDLEELRK RGMDEEVVQA ADEGTVVLGV CGGYQMLGRE LVDESGGELD PGESVPGLGL
LDAVTVFPSD AGKVTVRSEG VVNHPHLRGI RVEGFEIHEG RTYTDEPHLV RLRSGYGNRG
CFLDGAYRTD RPVLGTYLHG IFFNRRFRHE FLRWVSGGRW KPPERDVVRE AVKRNLQVAL
EIVESTDLPE LLGE