COBQ_VIBC1
ID COBQ_VIBC1 Reviewed; 475 AA.
AC A7N8K5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, 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};
GN OrderedLocusNames=VIBHAR_05724;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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; CP000790; ABU73618.1; -; Genomic_DNA.
DR AlphaFoldDB; A7N8K5; -.
DR SMR; A7N8K5; -.
DR EnsemblBacteria; ABU73618; ABU73618; VIBHAR_05724.
DR KEGG; vha:VIBHAR_05724; -.
DR PATRIC; fig|338187.25.peg.4550; -.
DR OMA; GREVHDP; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008152; Chromosome II.
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.
FT CHAIN 1..475
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332400"
FT DOMAIN 244..431
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 325
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 475 AA; 51326 MW; E45284D7E8E5C6ED CRC64;
MVQGTTSDAG KSVLVAGLCR VLARKGIKVA PFKPQNMALN SAVTKDGGEI GRAQAVQAQA
CNVEPTVHMN PVLIKPNSDT GAQIILQGKA LSNMDAVGFH DYKRVAMGTV LDSFAKLTDE
YESVMIEGAG SPAEINLREN DIANMGFAEE ADVPVIIIAD IDRGGVFAHL YGTLALLSES
EQARVKGFVI NRFRGDIGLL ESGLDWLEEK TGKPVLGVLP FLHGLNLEAE DAITAEQELS
SQVKLNVVVP VLTRISNHTD FDVLRLNPDI NLRYVGKGEK IDKADLVILP GTKSVRDDLD
YLRSQGWDKD IQRHIRLGGK VIGICGGYQM LGKLIDDPNG VEGSPGKSEG LGLLDITTTL
TDSKQLTNTH AQLCLNGKTA NVKGYEIHVG RSEVQGAQPL RLSSGEAEGA ISECGQIMGT
YLHGFFDEAD VLSLVSEWVN GTQIKQQDFE QLKEKGINRI ADAIAQHMNL DFLFK
