COBQ_LISMF
ID COBQ_LISMF Reviewed; 511 AA.
AC Q720M1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=LMOf2365_1217;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT03993.1; -; Genomic_DNA.
DR RefSeq; WP_003734682.1; NC_002973.6.
DR AlphaFoldDB; Q720M1; -.
DR SMR; Q720M1; -.
DR KEGG; lmf:LMOf2365_1217; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
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..511
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141307"
FT DOMAIN 251..443
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 511 AA; 56278 MW; E3C1A3A56EDECA93 CRC64;
MVKQIMIQGT ASDAGKSVLV AGLCRLFKNK GKRVVPFKSQ NMSLNSFITA TGDEMGRAQV
FQAEAAGVFP DVRMNPVLLK PTNDRQSQVI FMGAILDNMD AVTYHDFKQT LIPKIQAVYQ
SLADENDIIV LEGAGSPAEI NLNDRDIVNM GMAKMVDAPV VLVADIDKGG VFASIYGTIM
LLNEEERARI KGVIINKFRG DVALLQPGID MIEELTNVPV IGVIPYANLQ LEEEDSVSLS
GKNYVPDSNA LLDIAIICLP RISNFTDFHS LEIQPEISLR YIRNLADFGK PDLVIIPGSK
NTLEDMAFLE ESGLKKAIQN FAENAGKVIG ICGGYQMLGK KMLDPNQVES KQLEIAGLGL
LDTETIFLDQ KRTTQITGVT HSGEAVEGYE IHMGETKRGE STSPFCEIKA VNGNEETHQD
GAISVNKNII GTYIHGIFDN DVFLGNLFDE LLTRKNKSVY PHEIINLKEH KEQEYDKLAA
LLEANIQMDQ LEKIMKGEKI CVSTQKPAIK E