COBQ_SYNPW
ID COBQ_SYNPW Reviewed; 494 AA.
AC A5GMB9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=SynWH7803_1658;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-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; CT971583; CAK24084.1; -; Genomic_DNA.
DR RefSeq; WP_011933556.1; NC_009481.1.
DR AlphaFoldDB; A5GMB9; -.
DR SMR; A5GMB9; -.
DR STRING; 32051.SynWH7803_1658; -.
DR EnsemblBacteria; CAK24084; CAK24084; SynWH7803_1658.
DR KEGG; syx:SynWH7803_1658; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001566; 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; 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; Reference proteome.
FT CHAIN 1..494
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332397"
FT DOMAIN 248..445
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 437
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 494 AA; 54279 MW; 7FA1C0CBD8D6E983 CRC64;
MVLGTSSGAG KSLMTAALCR VLKRRGETPL PFKGQNMSNN AWVDPGGGEM AYSQALQAWA
AGREPECAMN PVLLKPQGDS TSEVIHLGRS VGTCRAEHYY RDWFRPGWAA IRQGLHTLEN
ENPEGRLVLE GAGSPVEVNL QARDLTNLRL AQYLRARCLL VADIERGGVF AQIVGTLALL
RPVERPLISG LLINRFRGRR ELFDEGRRWL EQHTGIPVLG VMPWLDELFP PEDSLDLLER
RGRKRGAELE IAVLKLPSLS NFSDLDPLEA EPTVQLRWVA PGEPLGTPDA VVIPGSKQTL
RDLGRLHSSG LGSAVQRFAR SGGAVFGVCG GMQMLGQELE DPEGLEGQAA AGGNGAMTGL
GLLPLRTRFG GEKALRHRQS SVHWPEHQPT LSVEGFELHR GHTHALEPCS NLCEDPSLGW
VARCGDQGGI AAGTYLHGIF DNGPWRRRWL NQLRIRRGLE LLSEQQPHHS RQRDALLDRL
ADAFETHVNL EPLL
