COBQ_BRADU
ID COBQ_BRADU Reviewed; 482 AA.
AC Q89Q71;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=bll3259;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC48524.1; -; Genomic_DNA.
DR RefSeq; NP_769899.1; NC_004463.1.
DR RefSeq; WP_011086043.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89Q71; -.
DR SMR; Q89Q71; -.
DR STRING; 224911.27351518; -.
DR EnsemblBacteria; BAC48524; BAC48524; BAC48524.
DR GeneID; 64023009; -.
DR KEGG; bja:bll3259; -.
DR PATRIC; fig|224911.44.peg.2904; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR InParanoid; Q89Q71; -.
DR OMA; EIHHGVA; -.
DR PhylomeDB; Q89Q71; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002526; 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..482
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141289"
FT DOMAIN 249..436
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 428
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 482 AA; 51280 MW; D455C166E384AA05 CRC64;
MARALMIQGA GSDVGKSLIV AGLARAFTRR GLRVLPFKPQ NMSNNAAVTV DGGEIGRAQA
LQALAAGVEP HTDMNPVLLK PETDVGAQVV VHGKRIATAR AREYAAMKPS LMGAVLESFE
RLKARADLVL VEGAGSPAEV NLRKADIANM GFARKADVPV VLIGDIDRGG VIAQLVGIKT
VIDPDDAAMI QGFVINKFRG DPTLFDDGYK LIEAKTAWRG FGVLPWFARA GELPAEDALG
LSDARKPGQC KIACLALSRI ANFDDLDPLK LEAAVDLVMV RPGEAIPGDV RLVIIPGSKS
TRGDLAFLRA QGWDIDLLAH YRRGGHVLGL CGGYQMLGRS VADPDGIEGP AGDTPGLGLL
DVQTVMSPQK TLTRVTAVHA ATNQPIQAYE IHIGRTDGPD RARPFAKLNG EPEGAISSDG
RVQGSYLHGL FTSDDFRKAF LTKLDIPAGD EPYHSRVESA LDALADHIEK HLDVEGLLSL
AR