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Database: UniProt
Entry: L7EC95_MICAE
LinkDB: L7EC95_MICAE
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ID   L7EC95_MICAE            Unreviewed;       491 AA.
AC   L7EC95;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN   ECO:0000313|EMBL:ELP57060.1};
GN   ORFNames=O53_1672 {ECO:0000313|EMBL:ELP57060.1};
OS   Microcystis aeruginosa TAIHU98.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=1134457 {ECO:0000313|EMBL:ELP57060.1, ECO:0000313|Proteomes:UP000010932};
RN   [1] {ECO:0000313|EMBL:ELP57060.1, ECO:0000313|Proteomes:UP000010932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAIHU98 {ECO:0000313|EMBL:ELP57060.1,
RC   ECO:0000313|Proteomes:UP000010932};
RX   PubMed=23766403;
RA   Yang C., Zhang W., Ren M., Song L., Li T., Zhao J.;
RT   "Whole-Genome Sequence of Microcystis aeruginosa TAIHU98, a Nontoxic Bloom-
RT   Forming Strain Isolated from Taihu Lake, China.";
RL   Genome Announc. 1:e00333-13(2013).
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:0000256|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELP57060.1}.
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DR   EMBL; ANKQ01000001; ELP57060.1; -; Genomic_DNA.
DR   RefSeq; WP_002734473.1; NZ_ANKQ01000001.1.
DR   AlphaFoldDB; L7EC95; -.
DR   PATRIC; fig|1134457.3.peg.1667; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000010932; Unassembled WGS sequence.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05389; CobQ_N; 1.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00028};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00028}; Ligase {ECO:0000313|EMBL:ELP57060.1}.
FT   DOMAIN          4..233
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          252..438
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   491 AA;  53849 MW;  38CC5CB053BFAF8A CRC64;
     MKAIMVVGTT SHAGKSFLTA ALCRLFNRKG WQVTPFKGQN MALNAYVTAG GEEMGHAQAV
     QAWAAGTVPR VEMNPILLKP QGNMTSQVII KGKAVGVTTA ADYYQNYFDQ GWQAIKESLA
     KLSAEFDLVV CEGAGSPAEI NLKHRDLTNM RVAKYLDAAT ILVVDIDRGG AFAHIVGTLE
     LLEPEERALI KGIVINKFRG QKSLLDSGIT WLEDYTKIPV LGVLPYSDIF LSAEDSLSLL
     DRPAQKPKAE LNISVIRLPH IANFTDFDPL CGEATVNVRY LELQESLGDP DGVIIPGSKT
     TVTDLIALNQ SGMANQLQAY HQKGGIIFGI CGGLQMLGRL ILDPDHREGP DSEAAGLNLL
     PLKTVITAEK ITRQRQVLSN YPQGGLPVTG YEIHQGISAW ESESGYQKMF EEDASLGIVS
     DSLSIWGCYL HGIFDNGSWR RTWLNHLRQR RGLLSLPTGI ANYSEQREIT LDNMANLLEE
     HLNLKPIFAH L
//
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