COBQ_PSEP1
ID COBQ_PSEP1 Reviewed; 484 AA.
AC A5W7Q6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Pput_4042;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
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., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-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; CP000712; ABQ80166.1; -; Genomic_DNA.
DR RefSeq; WP_012053449.1; NC_009512.1.
DR AlphaFoldDB; A5W7Q6; -.
DR SMR; A5W7Q6; -.
DR STRING; 351746.Pput_4042; -.
DR EnsemblBacteria; ABQ80166; ABQ80166; Pput_4042.
DR KEGG; ppf:Pput_4042; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
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.
FT CHAIN 1..484
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332373"
FT DOMAIN 248..435
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 484 AA; 51687 MW; 74DDFCE937FADC35 CRC64;
MTTLMVQGTT SDAGKSTLVT ALCRWLLRQG VAVVPFKPQN MALNSAVTAD GGEIGRAQAV
QAQACRLQPH TDMNPVLLKP NSDTGAQVII HGRAVTSMNA VAYHDYKTTA MQAVLASHQR
LSAAYPVVMV EGAGSPAEIN LRAGDIANMG FAEAVDCPVI LVADINRGGV FAHLVGTLEL
LSTTEQARVK GFVINRFRGD IALLQPGLDW LEQRTGKPVL GVLPYVTDLH LEAEDGIDVR
QGVKHARVLK VIVPVLPRIS NHTDFDPLRL HSQVDLQFIG PGQPIPAADL IILPGSKSVR
GDLAQLRERG WDKAIERHLR YGGKLIGICG GLQMLGREVH DPLGLEGAAG SSQGLGLLDY
ATVLEAEKQL RNVAGTLSLE AATVTGYEIH AGVTTGPALA QPAVQLADGR HDGAVSADDQ
ILATYLHGLF EGSQSCAALL RWAGLEDVQV IDYEALREHD IERLADLVEK HLDTAQLRQL
CGVA