COBQ_HALS3
ID COBQ_HALS3 Reviewed; 512 AA.
AC B0R5X2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=OE_3246F;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774415; CAP14139.1; -; Genomic_DNA.
DR RefSeq; WP_010903150.1; NC_010364.1.
DR AlphaFoldDB; B0R5X2; -.
DR SMR; B0R5X2; -.
DR EnsemblBacteria; CAP14139; CAP14139; OE_3246F.
DR GeneID; 5953653; -.
DR KEGG; hsl:OE_3246F; -.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR PhylomeDB; B0R5X2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001321; 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.
FT CHAIN 1..512
FT /note="Probable cobyric acid synthase"
FT /id="PRO_1000090228"
FT DOMAIN 275..460
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 452
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 512 AA; 52315 MW; 23CED7EDD38F34AF CRC64;
MTAGEDCRTI LVAGTASHVG KSTVAAGLCR LLADRGLSVA PFKAQNMSNN ARAVPVADGA
PPAADPWGEI GVSQYVQARA ARTAASTDHN PVLLKPRGDA ESQLVVDGRA VGHYSAGSYY
ESHWADARDA AAAAHARLAA DNDVVVAEGA GSIAELNLHD RDLANLETAR FADATILLVV
DIERGGAFAS LHGTLALLPD DIRDRVAGAV ITKFRGDRSL LDPGITEIEA RTGVPVLGVI
PHDDPGLPAE DSVSLPDPSE RVVDGGQDGV PDAASVTVAV PHLPHISNFT DLAPLARTPG
VRVAYQPLDA PLAAADAVVL PGTKNTVDDL RAAREAGLGR ALRAFDGPIV GLCGGYQMLG
DRITDAATES TADDLGAVDG VGVLPVETAF QPDKRVEAVT RELADCGALG GATGAVTGYE
IHMGRTTVPD GVPQPVGPAS AARGRVLGTY LHGLFGNDAA RRGFRDAVFA AAGVEQPAPA
DTPDQSPSDA AAALVDAHVD LDPLGVPPAP DA