COBQ_GLOC7
ID COBQ_GLOC7 Reviewed; 495 AA.
AC B7KHS7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=PCC7424_3640;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001291; ACK72024.1; -; Genomic_DNA.
DR RefSeq; WP_015955617.1; NC_011729.1.
DR AlphaFoldDB; B7KHS7; -.
DR SMR; B7KHS7; -.
DR STRING; 65393.PCC7424_3640; -.
DR PRIDE; B7KHS7; -.
DR EnsemblBacteria; ACK72024; ACK72024; PCC7424_3640.
DR KEGG; cyc:PCC7424_3640; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002384; 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..495
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116433"
FT DOMAIN 249..443
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 54283 MW; 615B2C7D6E809AA9 CRC64;
MKAIMVVGTT SHAGKSFLTT ALCRILARRG WHVTPFKGQN MALNSYVTPT GGEMGFAQAV
QAWAAGTAPR VEMNPILLKP QGNMTSQVIL MGKVAGQTTA SDYYEQYFKP GWEAIASALK
RLAFEYDLVI CEGAGSPAEI NLKHRDLTNM RVAQHLGATT LLVVDIDRGG AFAHVVGTLA
LLDPEERALI KGIIINKFRG QRSLLDSGIK WLEDYTGIPV LGVIPWSEIL FPAEDSLDLF
ERKTKPNGEI NINVIRLPRI SNFTDFDALE SEPTVSLNYL DLSQELGYPD AVIIPGSKTT
IQDLSALHTS GMAEKLEQYA NAGGIVLGIC GGFQMLGRRV LDPNQIEGKQ EEFAGLNLLP
IETTILPDKI TTQRQVFSNH PQSGLPVTGY EIHQGITRLA DGVKNLENVG CQALFNDEKL
GIVTHSQLVW GCYLHGLFDN GAWRRAWLNF LRHRRGLSAL PTGIPNYREQ REATLNSVAD
LVEANVNLSP ILSQL
