COBQ_CHLPD
ID COBQ_CHLPD Reviewed; 505 AA.
AC A1BFI0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Cpha266_1117;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
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; CP000492; ABL65157.1; -; Genomic_DNA.
DR RefSeq; WP_011744983.1; NC_008639.1.
DR AlphaFoldDB; A1BFI0; -.
DR SMR; A1BFI0; -.
DR STRING; 290317.Cpha266_1117; -.
DR EnsemblBacteria; ABL65157; ABL65157; Cpha266_1117.
DR KEGG; cph:Cpha266_1117; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_10; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008701; 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..505
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332327"
FT DOMAIN 260..453
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 341
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 445
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 505 AA; 54532 MW; ABF20459E2CAB5C2 CRC64;
MVNSSPVPGA LAIFGTASDV GKSIVATALC RMFSNAGIDV APYKAQNMSN NSGVTPDGCE
IGRAQIAQAE AARVVPTADM NPVLLKPNSD TGAQIVLQGK VCSTETAKGY FLDTSLWAEA
ARKSLDQLMQ RHELVVIEGA GSCAEMNLYD RDFVNFRTAR ISGAPVILVA DIDRGGVFAQ
VVGTLAVLPP EDRALVKGVI INRFRGDIDL FRDGVKLIET LAGIPVLGVI PYFRGFRIDA
EDAVPLSSKV DPSGAPEKGR IAVAAIYFPH ISNFTDLSPL ELDPKVELHY LHFPRSLRGY
QALILPGTKN VRGDLDWLTS LGWAEKIREF RRDGGLIMGI CGGYQMLGAT IADPSGVEGE
PGESAGLGML PVHTVLEEEK CLSNAIGNIQ GESIAVSGYE IHMGRTTSNG DCSSFLRVTA
RNNRPADDVD GVITPDGKVI GTYFHGIIDE PEVRCWFLRQ IDPAYTPDAE ERGRQESYDL
LADHFSGYLD IPKLYEIIQR PCPNP