COBQ_MICAN
ID COBQ_MICAN Reviewed; 491 AA.
AC B0JHX2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=MAE_57120;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009552; BAG05534.1; -; Genomic_DNA.
DR RefSeq; WP_012267957.1; NC_010296.1.
DR AlphaFoldDB; B0JHX2; -.
DR STRING; 449447.MAE_57120; -.
DR PaxDb; B0JHX2; -.
DR EnsemblBacteria; BAG05534; BAG05534; MAE_57120.
DR KEGG; mar:MAE_57120; -.
DR PATRIC; fig|449447.4.peg.5221; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR BioCyc; MAER449447:MAE_RS24890-MON; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001510; 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..491
FT /note="Cobyric acid synthase"
FT /id="PRO_1000074401"
FT DOMAIN 250..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 491 AA; 53963 MW; B4B3B46DBC2C99FF CRC64;
MKAIMAVGTT SHAGKSFLTA ALCRLFNRKG WQVTPFKGQN MALNAYVTAG GGEMGHAQAV
QAWAAGTIPR VEMNPILLKP QGNMTSQVII KGKAVGVTTA VDYYQNYFEQ GWQAIKESLA
KLSAEFDLVV CEGAGSPAEI NLKHRDLTNM RVAKYLDAAT ILVVDIDRGG AFAHVVGTLE
LLEPEERALI KGIVINKFRG QKSLLDSGIT WLEDYTKIPV LGVLPYSDIF LSAEDSLSLL
DRPAQKPKAE LNIIVIRLPH IANFTDFDPL CGEATVNVRY LELQESLGDP DGVIIPGSKT
TVADLIALNQ SGMANQLQAY HQRGGIIFGI CGGLQMLGRL ILDTDHREGP ESEAAGLNLL
PLKTVITAEK ITRQRQVLSN YPQGGLPVMG YEIHQGISQW ESESGYQKMF EEDASLGIVN
DSLSIWGCYL HGIFDNGSWR RTWLNHLRQR RGLLSLPTGI ANYCEQREIT LDNMANLLEE
HLNLQPIFAH L