COBQ_JANMA
ID COBQ_JANMA Reviewed; 476 AA.
AC A6SWZ4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=mma_1101;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(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}.
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DR EMBL; CP000269; ABR89064.1; -; Genomic_DNA.
DR RefSeq; WP_012078958.1; NC_009659.1.
DR AlphaFoldDB; A6SWZ4; -.
DR SMR; A6SWZ4; -.
DR STRING; 375286.mma_1101; -.
DR EnsemblBacteria; ABR89064; ABR89064; mma_1101.
DR KEGG; mms:mma_1101; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_4; -.
DR OMA; GREVHDP; -.
DR OrthoDB; 744477at2; -.
DR BioCyc; JSP375286:MMA_RS05720-MON; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006388; 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..476
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332343"
FT DOMAIN 242..428
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 420
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 476 AA; 50863 MW; 7BF3A01F78328A37 CRC64;
MVQGTTSDAG KTTLVAALCR LLAQEGVRVV PFKPQNMALN SAVTADGGEI GRAQALQAVA
AGLQPHTDMN PILLKPSSDT GAQVIIHGKA RSDMNARDYH AYKPIAMQAV LESYQRLQTQ
YESVLVEGAG SPAEVNLRER DIANMGFAEA VDCPVILVAD IDRGGVFAHI IGTLACLSES
ERRRTVGFVI NRFRGDISLL EPGLKWLEEQ TGKPVLAVLP YLHGLFLDAE DAVEHTQAVR
GAFRVVVPVP PRISNHTDFD ALRAHPEIDL QLVGPGQPIP AADLIILPGS KNTRGDLEWL
IANGWREALL RHLRYGGKII GICGGYQMLG MTVADPHGVE GTPGESAGLG LLDVATELTR
DKRLEQVSGV CAFADVGVSG YEIHMGTSDG AARAQPAFLI DGRPEGARSA DDQVLGTYLH
GLFDTPDACA ALLHWAGLNS DVRVDTAQLR EASLQRLAAA ARPLLAALRA LPDYSR