COBQ_XANP2
ID COBQ_XANP2 Reviewed; 488 AA.
AC A7ILW0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Xaut_3778;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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; CP000781; ABS69003.1; -; Genomic_DNA.
DR RefSeq; WP_012115750.1; NC_009720.1.
DR AlphaFoldDB; A7ILW0; -.
DR SMR; A7ILW0; -.
DR STRING; 78245.Xaut_3778; -.
DR PRIDE; A7ILW0; -.
DR EnsemblBacteria; ABS69003; ABS69003; Xaut_3778.
DR KEGG; xau:Xaut_3778; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR PhylomeDB; A7ILW0; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002417; 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..488
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090254"
FT DOMAIN 252..442
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 488 AA; 50840 MW; DD055DEE2C6ED5DF CRC64;
MARALMFQGT GSDVGKSLLV AGLARAFTLR GLKVRPFKPQ NMSNNAAVTA DGGEIGRAQA
LQARAARVPL SVHMNPVLLK PQGETGAQVV VQGRVHGTAK AAAYQGMKPS LLPFVLDSFD
RLKAEADLVL VEGAGSASEV NLRTGDIANM GFARAADVPV VVIGDIDRGG VIASLVGTKA
VIDAADAALI KGFVVNRFRG DPSLFATGME LIARQTGWAA LGLVPHFSEA IRLPAEDALA
LSAPPAPKPR ARTRICVPIL PHVSNFDDLD PLDAEPSVEV RRIRPHETLP VDTDLVLLIG
SKATIADLAA LKAEGLHHDI LAFARRGGHV MGLCGGYQML GETIADPDGI EGEAKIARGL
GLLKVHTVLS PEKRLVEVAG VALDPAVAAP FSGYEMHMGV TAGADAEQPF AVLSDGRQDG
ARSASGRVSG TYVHGLFASD AFRSGLLGAL GGAPSQAAYE QGVEETLDRL AAHLAAHLDL
DLLFSLAR