COBQ_BEII9
ID COBQ_BEII9 Reviewed; 488 AA.
AC B2IE16;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Bind_0387;
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT 9039.";
RL Submitted (MAR-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}.
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; CP001016; ACB94040.1; -; Genomic_DNA.
DR AlphaFoldDB; B2IE16; -.
DR SMR; B2IE16; -.
DR STRING; 395963.Bind_0387; -.
DR EnsemblBacteria; ACB94040; ACB94040; Bind_0387.
DR KEGG; bid:Bind_0387; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001695; 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..488
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116432"
FT DOMAIN 254..442
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 488 AA; 52519 MW; DDFFE037DF17BF50 CRC64;
MAKALMLQGT GSDVGKTLIV AGLCRAYMRR GLRVRPFKPQ NMSNNAAVTL DGGEIGRAQA
LQAQACGVPP SVHMNPVLLK PQSGTGSQII LQGRLSGQAE ARTYQAMKKH WLAIVLESFQ
HLKDEADLVL VEGAGSASEI NLRANDIANM GFARAADVPV IVIGDIDRGG VIAQIAGTKL
VITPQDAEMV VGFLVNRFRG DPDLFKEGMR QIEHFSGWRG LGLIPHCPAA RDLPAEDAMA
LGRHLNGERS AHTKFKIVVP VLPGIANFDD LDPLRMERGV ELIMIRPGTY LPVEADLVLL
IGSKTTIADL VAFREAGWDV DLAAYVRRGG KVFGLCGGYQ MLGENLRDPL GLEGPPSEVR
GLGLLALETV FTQEKTLVAV EGVSLPDEVP FTGFEMHVGH TSGDDCARPF LRLTDGRQDG
AVSKDGRIAG CYVHGLFGMD TQRRAFLARF GVAAGDFSYL EKVEAALDAV ADHLAQHIDL
DHLLTLAR
