COBQ_NOSP7
ID COBQ_NOSP7 Reviewed; 494 AA.
AC B2J764;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Npun_F0495;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) 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; CP001037; ACC79272.1; -; Genomic_DNA.
DR RefSeq; WP_012407297.1; NC_010628.1.
DR AlphaFoldDB; B2J764; -.
DR SMR; B2J764; -.
DR STRING; 63737.Npun_F0495; -.
DR EnsemblBacteria; ACC79272; ACC79272; Npun_F0495.
DR KEGG; npu:Npun_F0495; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR PhylomeDB; B2J764; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001191; 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_1000090237"
FT DOMAIN 252..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 494 AA; 54343 MW; E82E1B036F2A96CF CRC64;
MKSIMVVGTT SHAGKSLLTT AICRILSRRG WRVAPFKGQN MALNAYVTAS GGEIGYAQAV
QAWAAGVVPW VEMNPILLKP QGDMTSQVII KGRSVGKVSA SDYYEQYFEL GWRTIEESLQ
HLGTEFDLLV CEGAGSPAEI NLKHRDLTNM RVAKYLNAPT MLVVDIDRGG AFAHVVGTLE
LLEPDERALI KGVVINKFRG QRSLLDPGIK WLEERTGIPV IGVIPYLQEV FSTEDSLDLL
ERQSSSSKAQ TDLNIAVIRL PRIANFTDFD PLESESTVSV KYLSPKQDLG HPDAVIIPGT
KTTIADLLLL QKSGMAEAIQ HYAASGGTVL GICGGYQMLG QIIADPEGIE GQAGRFQGLN
LLPIRTVITG QKIARQRQVS SNYPQQGLPV NGFEIHQGRS RIEQQGIDPQ SYHALFDDIN
LGLVDSCQSV WGSYLHGLFD NGPWRRAWLN RLRQQRGLKS LPTGVANYRE QREQILDSLA
TEVESHLDLT PFLS