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
//