COBQ_STRSV
ID COBQ_STRSV Reviewed; 499 AA.
AC A3CL74;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=SSA_0481;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN43929.1; -; Genomic_DNA.
DR RefSeq; WP_011836536.1; NC_009009.1.
DR RefSeq; YP_001034479.1; NC_009009.1.
DR AlphaFoldDB; A3CL74; -.
DR SMR; A3CL74; -.
DR STRING; 388919.SSA_0481; -.
DR PRIDE; A3CL74; -.
DR EnsemblBacteria; ABN43929; ABN43929; SSA_0481.
DR KEGG; ssa:SSA_0481; -.
DR PATRIC; fig|388919.9.peg.465; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002148; 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; 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; Reference proteome.
FT CHAIN 1..499
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002379"
FT DOMAIN 251..442
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 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 499 AA; 55586 MW; 401D5D847DD47AF0 CRC64;
MVKALMVQGT ASDAGKSIIA AGLCRIFKQD GLEVVPFKSQ NMALNSFITK KGDEMGRAQV
VQAEAAGKEP DVRMNPVLLK PTSDRKSQVV FLGRVLRDMD AVEYHEYKQQ LLPKIKEVYD
ELGAENDIIV IEGAGSPAEI NLNDRDIVNM GMAKLVDAPV ILVADIDKGG VFASIYGTIE
LMPPEDRKRI KGVIINKFRG DVALLQSGID MIEELTQVPV IGVVPYAQLD IDSEDSVALV
QKSRRFDSRK SLDIAVVSLK RLSNFTDFHS LEIQPDVSVR YVQPGDAIGR PDLLILPGSK
NTIEDMNYLC ESGLEAEILE CLEQGVRIFG ICGGYQLLGQ KISDPLHLES DLEETRGLGI
LETETVLQPV KRTTQVRALH EGQELEGYEI HMGETQLADR LEPFSIIKEQ NGEATERPDG
AVAYGGQVQG TYLHGVFDNL EWTRQYLNEL RLAKGLEPLE DQLVSIKDFK DREYDKLADV
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