COBQ_CHLSY
ID COBQ_CHLSY Reviewed; 489 AA.
AC B9LKN1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Chy400_2767;
OS Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=480224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29364 / DSM 637 / Y-400-fl;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus sp. Y-400-fl.";
RL Submitted (JAN-2009) 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; CP001364; ACM54156.1; -; Genomic_DNA.
DR RefSeq; WP_012258419.1; NC_012032.1.
DR AlphaFoldDB; B9LKN1; -.
DR KEGG; chl:Chy400_2767; -.
DR HOGENOM; CLU_019250_2_2_0; -.
DR OMA; DVRMNPL; -.
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..489
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116900"
FT DOMAIN 251..444
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 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 489 AA; 52814 MW; 3D1CC9C3D349B75E CRC64;
MQAPVLMVVG TASSVGKSTL VTALCRLAYR RGLRVAPFKA QNMSNNAAVT ADGKEIARST
AVQAAAAGIA PTVAMNPILI KPEGQRRSQI IVEGRPWQSL TATDFWQRKA QLWSVVTRNL
DHLRATYDLV IAEGAGSPVE LNLKPGDIVN MRVARYAQAQ TILVGDIDRG GIFAQLLGTL
MLLEPEERQL ITGCIVNRFR GDPSLFADGV TILEERSGLP VLGVIPWLDD LGLPEEDAVA
LEQPPVAPAH GLIIAVIRLP TIANFDDFDP LAREPGVVVR YIDHPLELTG AAAVILPGVK
HTLAARHWLH ERGFDNALRE FTGAIVGICG GYQLLGERIS DPLAVEGSGG EAAGLGLLPI
ETIFTTAKQT TQTIACAQVP WAGNEPLQGY EIHMGQSYRR GEAPAFLRII QRGNTPTSAD
DGCISSDGRV WGCYLHGIFA NDTFRRGWLR RLGWQPPTTP VARADPFDRL ADHVAAALGP
AVLDRLMRR
