COBQ_TRIEI
ID COBQ_TRIEI Reviewed; 488 AA.
AC Q10XP0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Tery_3957;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
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 Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-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; CP000393; ABG52984.1; -; Genomic_DNA.
DR RefSeq; WP_011613314.1; NC_008312.1.
DR AlphaFoldDB; Q10XP0; -.
DR SMR; Q10XP0; -.
DR STRING; 203124.Tery_3957; -.
DR EnsemblBacteria; ABG52984; ABG52984; Tery_3957.
DR KEGG; ter:Tery_3957; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
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; 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.
FT CHAIN 1..488
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332399"
FT DOMAIN 250..438
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 430
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 488 AA; 53895 MW; A30B4FF3D77FC41B CRC64;
MKAIMVVGTT SHAGKSLITT AICRILSRRG WKVTPFKGQN MALNSYVTST GGEMGHAQAV
QAWAAGVTPA IEMNPILLKP QGDMTSQVII KGKASGTVGA VDYYQQYFDI GWNAIQESLE
TLSQEFNMIV CEGAGSPAEI NLKHRDLTNM RVAKHLNAST ILVVDIDRGG AFAHIIGTLE
LLEPEERNLI KGIVINKFRG QRSLLDSGIH WLEKKTNIPV IGVIPWINEA FPAEDSLSIL
EQRYNKHTTD ITIAIIRLPR ISNFTDFEPL EAESSVKIKY IHPNDSLGDP DAIIIPGTKT
TINDLLVLQK SGMAEAIKSY QSSGGIVMGI CGGFQMLGEV LIDSQGLEGK QGEYKGLELL
PLITTITPKK IASQRQVIAN YPLGNLPVIG YEIHQGRTIV TKPDIVKPLF NDYDLGFVDS
YDSIWGNYLH GIFDNGSWRR SWLNILRHKR GLNSLPTSIS NYREQREIIL DSIADKVNEH
LDLKPVLT
