COBQ_ACISJ
ID COBQ_ACISJ Reviewed; 493 AA.
AC A1WAM6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Ajs_3178;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
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; CP000539; ABM43301.1; -; Genomic_DNA.
DR RefSeq; WP_011806300.1; NC_008782.1.
DR AlphaFoldDB; A1WAM6; -.
DR SMR; A1WAM6; -.
DR STRING; 232721.Ajs_3178; -.
DR EnsemblBacteria; ABM43301; ABM43301; Ajs_3178.
DR KEGG; ajs:Ajs_3178; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_1_4; -.
DR OMA; DVRMNPL; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000645; 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..493
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332317"
FT DOMAIN 261..455
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 447
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 493 AA; 52200 MW; 2AC41564D3CD95FF CRC64;
MNKTRPGPAR CVMVLGTTSG AGKSWLATAL CRYYSNQGLK VAPFKAQNMS NNARVVAAPG
EQFGEIGSAQ YFQALAARAV PDVRMNPLLL KPEADTKSQV VLLGQVSDEL SQLPWRGRSQ
RVWPQIAAAL DALRAENDVV VIEGAGSPAE INLHASDVVN MRVARHAEAR CLLVTDIDRG
GAFAHLFGTW ALLPEEERAL IAGFVLNKFR GDEALLAPAP QMLQDKTGVP VVATIPMQWN
HGLPEEDGVF DMRSTAVGAV HTRIAVVAYP RISNLDEFQP LKNVPGVRLS WARSPADVEG
ADWIVLPGSK ATAADLAWLR AQGLDAAIAA HAARGGRVLG VCGGLQMLGE ALIDTVGVDG
NGPGLGLLPL VTSFEATKTV RPTRQCFGAV QGAWRHLAGV AVQGYEIHHG QTAQHPAMAA
SGDVARELMP GLAWQNPAGN VLGLYLHGLF EDAAVLRALF GADAPTLDAV FEGLAAGIAR
HFEPRALDAL AAQ
