COBQ_PARDP
ID COBQ_PARDP Reviewed; 477 AA.
AC A1B8D6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Pden_3713;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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; CP000490; ABL71780.1; -; Genomic_DNA.
DR RefSeq; WP_011749949.1; NC_008687.1.
DR AlphaFoldDB; A1B8D6; -.
DR SMR; A1B8D6; -.
DR STRING; 318586.Pden_3713; -.
DR PRIDE; A1B8D6; -.
DR EnsemblBacteria; ABL71780; ABL71780; Pden_3713.
DR KEGG; pde:Pden_3713; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; DVRMNPL; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000361; Chromosome 2.
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; 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; 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..477
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332358"
FT DOMAIN 248..432
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 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 477 AA; 50121 MW; E3F857395900FD22 CRC64;
MGALMIQGTG SNVGKSLLVA GLCRAARRRG IDVAPFKPQN MSNNAAVTPD GGEIGRAQAL
QARAAGLAPS VHMNPVLLKP ETDRAAQVVV QGRAATRAAA ADYGALKARL MGAVLDSFAR
LRTTHELVLV EGAGSPAEVN LRARDIANMG FARAADVPVV LAGDIDRGGV IAQIVGTQAV
IDPADAAMIR GFVINRFRGD PSLFDAGRRF IVERTGWPDL GLVPWFPDAV RLPAEDAVDL
RRASGGGGLH IACPMLSRIA NFDDLDPLAA EPAVRLSMVP PGHALPGDAD LVILPGTKST
RGDLAFLREQ GWDIDLAAHL RRGGRVLGIC GGYQMLGRMI HDPEGHDGSP GSTPGLGLLD
IETRMAPEKR LTRIAGRALG QPVEGYEIHM GRSEGPDCAR PFAHIPEPDG ATSPDGRVAG
TYLHGLFSGD GFRAAWLGQF GAASALDYGA GVDEVLDRLA GHLEAHLDID RLFALAR
